Genome-Wide Essentiality Analysis of Mycobacterium abscessus by Saturated Transposon Mutagenesis and Deep Sequencing
Mycobacterium abscessus is an emerging opportunistic human pathogen that naturally resists most major classes of antibiotics, making infections difficult to treat. Thus far, little is known about physiology, pathogenesis, and drug resistance. Genome-wide analyses have comprehensively catalogued gene...
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Published in | mBio Vol. 12; no. 3; p. e0104921 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
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American Society for Microbiology
29.06.2021
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Abstract | Mycobacterium abscessus is an emerging opportunistic human pathogen that naturally resists most major classes of antibiotics, making infections difficult to treat. Thus far, little is known about
physiology, pathogenesis, and drug resistance. Genome-wide analyses have comprehensively catalogued genes with essential functions in Mycobacterium tuberculosis and Mycobacterium avium subsp.
(here,
) but not in
. By optimizing transduction conditions, we achieved full saturation of TA insertion sites with Himar1 transposon mutagenesis in the
ATCC 19977
genome, as confirmed by deep sequencing prior to essentiality analyses of annotated genes and other genomic features. The overall densities of inserted TA sites (85.7%), unoccupied TA sites (14.3%), and nonpermissive TA sites (8.1%) were similar to results in
and
. Of the 4,920 annotated genes, 326 were identified as essential, 269 (83%) of which have mutual homology with essential
genes, while 39 (12%) are homologous to genes that are not essential in
and
, and 11 (3.4%) only have homologs in
. Interestingly, 7 (2.1%) essential
genes have no homologs in either
or
, two of which were found in phage-like elements. Most essential genes are involved in DNA replication, RNA transcription and translation, and posttranslational events to synthesize important macromolecules. Some essential genes may be involved in
pathogenesis and antibiotics response, including certain essential tRNAs and new short open reading frames. Our findings will help to pave the way for better understanding of
and benefit development of novel bactericidal drugs against
.
Limited knowledge regarding
pathogenesis and intrinsic resistance to most classes of antibiotics is a major obstacle to developing more effective strategies to prevent and mitigate disease. Using optimized procedures for Himar1 transposon mutagenesis and deep sequencing, we performed a comprehensive analysis to identify
genetic elements essential for
growth and compare them to similar data sets for
and
subsp.
. Most essential
genes have mutual homology with essential
genes, providing a foundation for leveraging available knowledge from
to develop more effective drugs and other interventions against
. A small number of essential genes unique to
deserve further attention to gain insights into what makes
different from other mycobacteria. The essential genes and other genomic features such as short open reading frames and noncoding RNA identified here will provide useful information for future study of
pathogenicity and new drug development. |
---|---|
AbstractList | Mycobacterium abscessus is an emerging opportunistic human pathogen that naturally resists most major classes of antibiotics, making infections difficult to treat. Thus far, little is known about
physiology, pathogenesis, and drug resistance. Genome-wide analyses have comprehensively catalogued genes with essential functions in Mycobacterium tuberculosis and Mycobacterium avium subsp.
(here,
) but not in
. By optimizing transduction conditions, we achieved full saturation of TA insertion sites with Himar1 transposon mutagenesis in the
ATCC 19977
genome, as confirmed by deep sequencing prior to essentiality analyses of annotated genes and other genomic features. The overall densities of inserted TA sites (85.7%), unoccupied TA sites (14.3%), and nonpermissive TA sites (8.1%) were similar to results in
and
. Of the 4,920 annotated genes, 326 were identified as essential, 269 (83%) of which have mutual homology with essential
genes, while 39 (12%) are homologous to genes that are not essential in
and
, and 11 (3.4%) only have homologs in
. Interestingly, 7 (2.1%) essential
genes have no homologs in either
or
, two of which were found in phage-like elements. Most essential genes are involved in DNA replication, RNA transcription and translation, and posttranslational events to synthesize important macromolecules. Some essential genes may be involved in
pathogenesis and antibiotics response, including certain essential tRNAs and new short open reading frames. Our findings will help to pave the way for better understanding of
and benefit development of novel bactericidal drugs against
.
Limited knowledge regarding
pathogenesis and intrinsic resistance to most classes of antibiotics is a major obstacle to developing more effective strategies to prevent and mitigate disease. Using optimized procedures for Himar1 transposon mutagenesis and deep sequencing, we performed a comprehensive analysis to identify
genetic elements essential for
growth and compare them to similar data sets for
and
subsp.
. Most essential
genes have mutual homology with essential
genes, providing a foundation for leveraging available knowledge from
to develop more effective drugs and other interventions against
. A small number of essential genes unique to
deserve further attention to gain insights into what makes
different from other mycobacteria. The essential genes and other genomic features such as short open reading frames and noncoding RNA identified here will provide useful information for future study of
pathogenicity and new drug development. Limited knowledge regarding Mycobacterium abscessus pathogenesis and intrinsic resistance to most classes of antibiotics is a major obstacle to developing more effective strategies to prevent and mitigate disease. Using optimized procedures for Himar1 transposon mutagenesis and deep sequencing, we performed a comprehensive analysis to identify M. abscessus genetic elements essential for in vitro growth and compare them to similar data sets for M. tuberculosis and M. avium subsp. hominissuis . Mycobacterium abscessus is an emerging opportunistic human pathogen that naturally resists most major classes of antibiotics, making infections difficult to treat. Thus far, little is known about M. abscessus physiology, pathogenesis, and drug resistance. Genome-wide analyses have comprehensively catalogued genes with essential functions in Mycobacterium tuberculosis and Mycobacterium avium subsp. hominissuis (here, M. avium ) but not in M. abscessus . By optimizing transduction conditions, we achieved full saturation of TA insertion sites with Himar1 transposon mutagenesis in the M. abscessus ATCC 19977 T genome, as confirmed by deep sequencing prior to essentiality analyses of annotated genes and other genomic features. The overall densities of inserted TA sites (85.7%), unoccupied TA sites (14.3%), and nonpermissive TA sites (8.1%) were similar to results in M. tuberculosis and M. avium . Of the 4,920 annotated genes, 326 were identified as essential, 269 (83%) of which have mutual homology with essential M. tuberculosis genes, while 39 (12%) are homologous to genes that are not essential in M. tuberculosis and M. avium , and 11 (3.4%) only have homologs in M. avium . Interestingly, 7 (2.1%) essential M. abscessus genes have no homologs in either M. tuberculosis or M. avium , two of which were found in phage-like elements. Most essential genes are involved in DNA replication, RNA transcription and translation, and posttranslational events to synthesize important macromolecules. Some essential genes may be involved in M. abscessus pathogenesis and antibiotics response, including certain essential tRNAs and new short open reading frames. Our findings will help to pave the way for better understanding of M. abscessus and benefit development of novel bactericidal drugs against M. abscessus . IMPORTANCE Limited knowledge regarding Mycobacterium abscessus pathogenesis and intrinsic resistance to most classes of antibiotics is a major obstacle to developing more effective strategies to prevent and mitigate disease. Using optimized procedures for Himar1 transposon mutagenesis and deep sequencing, we performed a comprehensive analysis to identify M. abscessus genetic elements essential for in vitro growth and compare them to similar data sets for M. tuberculosis and M. avium subsp. hominissuis . Most essential M. abscessus genes have mutual homology with essential M. tuberculosis genes, providing a foundation for leveraging available knowledge from M. tuberculosis to develop more effective drugs and other interventions against M. abscessus . A small number of essential genes unique to M. abscessus deserve further attention to gain insights into what makes M. abscessus different from other mycobacteria. The essential genes and other genomic features such as short open reading frames and noncoding RNA identified here will provide useful information for future study of M. abscessus pathogenicity and new drug development. Mycobacterium abscessus is an emerging opportunistic human pathogen that naturally resists most major classes of antibiotics, making infections difficult to treat. Thus far, little is known about M. abscessus physiology, pathogenesis, and drug resistance. Genome-wide analyses have comprehensively catalogued genes with essential functions in Mycobacterium tuberculosis and Mycobacterium avium subsp. hominissuis (here, M. avium ) but not in M. abscessus . By optimizing transduction conditions, we achieved full saturation of TA insertion sites with Himar1 transposon mutagenesis in the M. abscessus ATCC 19977 T genome, as confirmed by deep sequencing prior to essentiality analyses of annotated genes and other genomic features. The overall densities of inserted TA sites (85.7%), unoccupied TA sites (14.3%), and nonpermissive TA sites (8.1%) were similar to results in M. tuberculosis and M. avium . Of the 4,920 annotated genes, 326 were identified as essential, 269 (83%) of which have mutual homology with essential M. tuberculosis genes, while 39 (12%) are homologous to genes that are not essential in M. tuberculosis and M. avium , and 11 (3.4%) only have homologs in M. avium . Interestingly, 7 (2.1%) essential M. abscessus genes have no homologs in either M. tuberculosis or M. avium , two of which were found in phage-like elements. Most essential genes are involved in DNA replication, RNA transcription and translation, and posttranslational events to synthesize important macromolecules. Some essential genes may be involved in M. abscessus pathogenesis and antibiotics response, including certain essential tRNAs and new short open reading frames. Our findings will help to pave the way for better understanding of M. abscessus and benefit development of novel bactericidal drugs against M. abscessus . Limited knowledge regarding Mycobacterium abscessusM. abscessusin vitroM. tuberculosisM. aviumhominissuis Mycobacterium abscessus is an emerging opportunistic human pathogen that naturally resists most major classes of antibiotics, making infections difficult to treat. Thus far, little is known about M. abscessus physiology, pathogenesis, and drug resistance. Genome-wide analyses have comprehensively catalogued genes with essential functions in Mycobacterium tuberculosis and Mycobacterium avium subsp. hominissuis (here, M. avium) but not in M. abscessus. By optimizing transduction conditions, we achieved full saturation of TA insertion sites with Himar1 transposon mutagenesis in the M. abscessus ATCC 19977T genome, as confirmed by deep sequencing prior to essentiality analyses of annotated genes and other genomic features. The overall densities of inserted TA sites (85.7%), unoccupied TA sites (14.3%), and nonpermissive TA sites (8.1%) were similar to results in M. tuberculosis and M. avium. Of the 4,920 annotated genes, 326 were identified as essential, 269 (83%) of which have mutual homology with essential M. tuberculosis genes, while 39 (12%) are homologous to genes that are not essential in M. tuberculosis and M. avium, and 11 (3.4%) only have homologs in M. avium. Interestingly, 7 (2.1%) essential M. abscessus genes have no homologs in either M. tuberculosis or M. avium, two of which were found in phage-like elements. Most essential genes are involved in DNA replication, RNA transcription and translation, and posttranslational events to synthesize important macromolecules. Some essential genes may be involved in M. abscessus pathogenesis and antibiotics response, including certain essential tRNAs and new short open reading frames. Our findings will help to pave the way for better understanding of M. abscessus and benefit development of novel bactericidal drugs against M. abscessus. IMPORTANCE Limited knowledge regarding Mycobacterium abscessus pathogenesis and intrinsic resistance to most classes of antibiotics is a major obstacle to developing more effective strategies to prevent and mitigate disease. Using optimized procedures for Himar1 transposon mutagenesis and deep sequencing, we performed a comprehensive analysis to identify M. abscessus genetic elements essential for in vitro growth and compare them to similar data sets for M. tuberculosis and M. avium subsp. hominissuis. Most essential M. abscessus genes have mutual homology with essential M. tuberculosis genes, providing a foundation for leveraging available knowledge from M. tuberculosis to develop more effective drugs and other interventions against M. abscessus. A small number of essential genes unique to M. abscessus deserve further attention to gain insights into what makes M. abscessus different from other mycobacteria. The essential genes and other genomic features such as short open reading frames and noncoding RNA identified here will provide useful information for future study of M. abscessus pathogenicity and new drug development. |
Author | Rifat, Dalin Kreiswirth, Barry N Chen, Liang Nuermberger, Eric L |
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BackLink | https://www.ncbi.nlm.nih.gov/pubmed/34126767$$D View this record in MEDLINE/PubMed |
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Cites_doi | 10.1128/genomeA.00550-16 10.1099/mic.0.2007/012153-0 10.1002/9780470123188.ch4 10.1128/AAC.04347-14 10.1093/gbe/evw001 10.1016/j.drudis.2016.11.006 10.1002/open.202000042 10.1128/jb.174.4.1213-1221.1992 10.1111/j.1365-2958.2007.06078.x 10.1007/978-1-4939-2398-4_6 10.1016/j.jgar.2019.05.016 10.1073/pnas.1419677112 10.1093/nar/gkz333 10.1371/journal.pone.0029306 10.1146/annurev.micro.57.030502.090820 10.2147/CMR.S10043 10.1371/journal.pcbi.1004401 10.1038/s41579-020-0331-1 10.1261/rna.7030704 10.1093/jac/dkw466 10.1128/AAC.00912-12 10.1111/mmi.13406 10.1128/AAC.01000-19 10.1128/cmr.15.4.716-746.2002 10.1016/j.tube.2013.09.007 10.3389/fmicb.2018.00649 10.3389/fmicb.2019.01524 10.1073/pnas.1514135112 10.1021/acs.biochem.5b00993 10.1128/IAI.00531-06 10.1093/molbev/msq297 10.1097/01.prs.0000153818.99552.cc 10.1128/CMR.10.1.1-18.1997 10.1128/AAC.43.1.181 10.1016/j.chembiol.2014.04.009 10.1073/pnas.0504068102 10.1016/j.micinf.2016.09.001 10.1128/AAC.01919-18 10.1128/mSystems.00402-19 10.1038/s41598-019-40922-x 10.3967/bes2020.047 10.1128/AAC.00685-12 10.1128/iai.71.7.3927-3936.2003 10.1111/j.1365-2958.2006.05491.x 10.1016/j.bmcl.2017.08.012 10.3390/microorganisms7030090 10.1128/mBio.00747-13 10.1073/pnas.1315860110 10.1128/AAC.01353-17 10.1128/mSystems.00976-20 10.3390/antibiotics8040261 10.1074/jbc.M113.475798 10.1371/journal.ppat.1000507 10.1016/j.bmc.2017.05.015 10.1073/pnas.0502248102 10.1164/rccm.200604-571ST 10.1186/s12929-020-00667-6 10.1186/s12864-016-2868-y 10.1126/science.aaf8156 10.1111/j.1574-6976.2007.00099.x 10.1016/j.resmic.2004.08.011 10.1128/AAC.02245-18 10.1073/pnas.1713195115 10.1186/1471-2164-15-359 10.1073/pnas.1907946116 10.1128/mBio.02133-16 10.1186/1471-2180-14-75 10.1128/AAC.01899-19 10.1128/AEM.01914-08 10.1128/AAC.00689-09 10.1534/g3.119.400737 10.1128/JB.00760-17 10.1038/nm.2120 10.1038/s41598-020-57845-7 10.1074/jbc.M117.811190 10.4161/rna.8.1.13346 10.3109/14756366.2014.959512 10.1371/journal.pone.0005660 10.1186/1471-2105-14-303 10.1128/JCM.02087-16 10.3390/ijms20235868 10.1128/AAC.01503-18 10.1128/mSystems.00070-19 10.1128/AAC.01225-17 10.1128/JB.01064-13 10.1016/j.hoc.2012.02.002 10.1073/pnas.1231432100 10.1038/75843 10.1016/S0959-440X(02)00385-8 10.1371/journal.pgen.1004084 10.1128/AAC.01275-08 10.1038/s41598-017-01184-7 10.1128/IAI.53.3.631-635.1986 10.1042/BST0351325 10.1107/S0907444913013085 10.1128/AAC.00866-17 10.1021/acsinfecdis.0c00025 10.7883/yoken.66.480 10.1021/acs.jmedchem.7b00582 10.1093/jac/dkt410 10.1107/S0907444913026371 10.1074/jbc.RA118.002241 10.1093/bioinformatics/btu170 10.1101/663559 |
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Keywords | transposon mycobacterium genetics deep sequencing gene disruption transposon sequencing (Tn-Seq) genomics Himar1 mutagenesis essentiality essential gene Mycobacterium abscessus |
Language | English |
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References | Cortes, M, Singh, AK, Reyrat, JM, Gaillard, JL, Nassif, X, Herrmann, JL (B7) 2011; 6 Degiacomi, G, Sammartino, JC, Chiarelli, LR, Riabova, O, Makarov, V, Pasca, MR (B5) 2019; 20 Rosenthal, IM, Tasneen, R, Peloquin, CA, Zhang, M, Almeida, D, Mdluli, KE, Karakousis, PC, Grosset, JH, Nuermberger, EL (B17) 2012; 56 Bitter, W, Houben, ENG, Bottai, D, Brodin, P, Brown, EJ, Cox, JS, Derbyshire, K, Fortune, SM, Gao, L-Y, Liu, J, Gey van Pittius, NC, Pym, AS, Rubin, EJ, Sherman, DR, Cole, ST, Brosch, R (B34) 2009; 5 Turner, KH, Wessel, AK, Palmer, GC, Murray, JL, Whiteley, M (B85) 2015; 112 Datta, P, Dasgupta, A, Singh, AK, Mukherjee, P, Kundu, M, Basu, J (B51) 2006; 62 Minato, Y, Gohl, DM, Thiede, JM, Chacón, JM, Harcombe, WR, Maruyama, F, Baughn, AD (B13) 2019; 4 Foreman, M, Gershoni, M, Barkan, D (B9) 2020; 5 Newman, MI, Camberos, AE, Clynes, ND, Ascherman, JA (B3) 2005; 115 Nash, KA, Brown-Elliott, BA, Wallace, RJ (B75) 2009; 53 Locher, CP, Jones, SM, Hanzelka, BL, Perola, E, Shoen, CM, Cynamon, MH, Ngwane, AH, Wiid, IJ, van Helden, PD, Betoudji, F, Nuermberger, EL, Thomson, JA (B40) 2015; 59 Long, JE, DeJesus, M, Ward, D, Baker, RE, Ioerger, T, Sassetti, CM (B102) 2015; 1279 Wu, M, Li, B, Guo, Q, Xu, L, Zou, Y, Zhang, Y, Zhan, M, Xu, B, Ye, M, Yu, F, Zhang, Z, Chu, H (B60) 2019; 19 Dupont, C, Viljoen, A, Dubar, F, Blaise, M, Bernut, A, Pawlik, A, Bouchier, C, Brosch, R, Guérardel, Y, Lelièvre, J, Ballell, L, Herrmann, J-L, Biot, C, Kremer, L (B46) 2016; 101 Wower, I, Kowaleski, MP, Sears, LE, Zimmermann, RA (B98) 1992; 174 Rizzi, M, Schindelin, H (B64) 2002; 12 Nagaraja, V, Godbole, AA, Henderson, SR, Maxwell, A (B37) 2017; 22 Miller, RA, Britigan, BE (B29) 1997; 10 Behra, PRK, Das, S, Pettersson, BMF, Shirreff, L, DuCote, T, Jacobsson, K-G, Ennis, DG, Kirsebom, LA (B67) 2019; 9 Kumar, A, Kumar, S, Kumar, D, Mishra, A, Dewangan, RP, Shrivastava, P, Ramachandran, S, Taneja, B (B59) 2013; 69 Cheng, YS, Sacchettini, JC (B89) 2016; 55 Santos, ARS, Gerhardt, ECM, Moure, VR, Pedrosa, FO, Souza, EM, Diamanti, R, Högbom, M, Huergo, LF (B63) 2018; 293 Kim, YS, Yang, C-S, Nguyen, LT, Kim, JK, Jin, HS, Choe, JH, Kim, SY, Lee, H-M, Jung, M, Kim, J-M, Kim, MH, Jo, E-K, Jang, J-C (B100) 2017; 19 Kloesges, T, Popa, O, Martin, W, Dagan, T (B96) 2011; 28 DeJesus, MA, Ambadipudi, C, Baker, R, Sassetti, C, Ioerger, TR (B15) 2015; 11 Pryjma, M, Burian, J, Kuchinski, K, Thompson, CJ (B61) 2017; 61 Choi, GE, Min, KN, Won, CJ, Jeon, K, Shin, SJ, Koh, WJ (B39) 2012; 56 Alderwick, LJ, Birch, HL, Mishra, AK, Eggeling, L, Besra, GS (B48) 2007; 35 Griffith, DE, Aksamit, T, Brown-Elliott, BA, Catanzaro, A, Daley, C, Gordin, F, Holland, SM, Horsburgh, R, Huitt, G, Iademarco, MF, Iseman, M, Olivier, K, Ruoss, S, von Reyn, CF, Wallace, RJ, Winthrop, K (B73) 2007; 175 Dragset, MS, Ioerger, TR, Loevenich, M, Haug, M, Sivakumar, N, Marstad, A, Cardona, PJ, Klinkenberg, G, Rubin, EJ, Steigedal, M, Flo, TH (B12) 2019; 4 DeJesus, MA, Ioerger, TR (B16) 2013; 14 Liao, D, Fan, Q, Bao, L (B31) 2013; 66 Reitzer, L (B26) 2003; 57 Kim, B-J, Cha, G-Y, Kim, B-R, Kook, Y-H, Kim, B-J (B70) 2019; 10 Johansen, MD, Herrmann, JL, Kremer, L (B2) 2020; 18 Gopalaswamy, R, Shanmugam, S, Mondal, R, Subbian, S (B45) 2020; 27 Medjahed, H, Reyrat, JM (B8) 2009; 75 Sarathy, JP, Gruber, G, Dick, T (B20) 2019; 8 Richard, M, Gutierrez, AV, Viljoen, AJ, Ghigo, E, Blaise, M, Kremer, L (B62) 2018; 9 Sha, W, Weng, XH, Xiao, HP, He, GJ (B18) 2003; 26 Franz, ND, Belardinelli, JM, Kaminski, MA, Dunn, LC, Calado Nogueira de Moura, V, Blaha, MA, Truong, DD, Li, W, Jackson, M, North, EJ (B79) 2017; 25 Wang, Z, Soni, V, Marriner, G, Kaneko, T, Boshoff, HIM, Barry, CE, Rhee, KY (B27) 2019; 116 Kumar, P, Chauhan, V, Silva, JRA, Lameira, J, d’Andrea, FB, Li, S-G, Ginell, SL, Freundlich, JS, Alves, CN, Bailey, S, Cohen, KA, Lamichhane, G (B55) 2017; 61 Xu, L, Dong, Z, Fang, L, Luo, Y, Wei, Z, Guo, H, Zhang, G, Gu, YQ, Coleman-Derr, D, Xia, Q, Wang, Y (B104) 2019; 47 Soroka, D, Dubée, V, Soulier-Escrihuela, O, Cuinet, G, Hugonnet, J-E, Gutmann, L, Mainardi, J-L, Arthur, M (B47) 2014; 69 Sassi, M, Drancourt, M (B72) 2014; 15 Beiko, RG, Harlow, TJ, Ragan, MA (B95) 2005; 102 Pandya, AN, Prathipati, PK, Hegde, P, Li, W, Graham, KF, Mandal, S, Drescher, KM, Destache, CJ, Ordway, D, Jackson, M, North, EJ (B81) 2019; 63 Ripoll, F, Pasek, S, Schenowitz, C, Dossat, C, Barbe, V, Rottman, M, Macheras, E, Heym, B, Herrmann, J-L, Daffé, M, Brosch, R, Risler, J-L, Gaillard, J-L (B14) 2009; 4 Bellinzoni, M, Buroni, S, Pasca, MR, Guglierame, P, Arcesi, F, De Rossi, E, Riccardi, G (B66) 2005; 156 Bolger, AM, Lohse, M, Usadel, B (B103) 2014; 30 Bryant, JM, Grogono, DM, Rodriguez-Rincon, D, Everall, I, Brown, KP, Moreno, P, Verma, D, Hill, E, Drijkoningen, J, Gilligan, P, Esther, CR, Noone, PG, Giddings, O, Bell, SC, Thomson, R, Wainwright, CE, Coulter, C, Pandey, S, Wood, ME, Stockwell, RE, Ramsay, KA, Sherrard, LJ, Kidd, TJ (B4) 2016; 354 Quan, S, Imai, T, Mikami, Y, Yazawa, K, Dabbs, ER, Morisaki, N, Iwasaki, S, Hashimoto, Y, Furihata, K (B76) 1999; 43 Matern, WM, Jenquin, RL, Bader, JS, Karakousis, PC (B11) 2020; 10 Stokes, SS, Vemula, R, Pucci, MJ (B42) 2020; 6 Amin, AG, Goude, R, Shi, L, Zhang, J, Chatterjee, D, Parish, T (B43) 2008; 154 Machowski, EE, Senzani, S, Ealand, C, Kana, BD (B49) 2014; 14 Naville, M, Ghuillot-Gaudeffroy, A, Marchais, A, Gautheret, D (B105) 2011; 8 Pandey, SD, Pal, S, Kumar, NG, Bansal, A, Mallick, S, Ghosh, AS (B53) 2018; 200 Chhotaray, C, Wang, S, Tan, Y, Ali, A, Shehroz, M, Fang, C, Liu, Y, Lu, Z, Cai, X, Hameed, HMA, Islam, MM, Surineni, G, Tan, S, Liu, J, Zhang, T (B71) 2020; 10 B74 Dumas, E, Christina Boritsch, E, Vandenbogaert, M, Rodríguez de la Vega, RC, Thiberge, J-M, Caro, V, Gaillard, J-L, Heym, B, Girard-Misguich, F, Brosch, R, Sapriel, G (B35) 2016; 8 Lee, S, Jeon, BY, Bardarov, S, Chen, M, Morris, SL, Jacobs, WR (B83) 2006; 74 Arora, D, Chawla, Y, Malakar, B, Singh, A, Nandicoori, VK (B50) 2018; 293 Brown-Elliott, BA, Wallace, RJ (B1) 2002; 15 Kozikowski, AP, Onajole, OK, Stec, J, Dupont, C, Viljoen, A, Richard, M, Chaira, T, Lun, S, Bishai, W, Raj, VS, Ordway, D, Kremer, L (B80) 2017; 60 Dupont, C, Viljoen, A, Thomas, S, Roquet-Banères, F, Herrmann, J-L, Pethe, K, Kremer, L (B21) 2017; 61 Brown-Elliott, BA, Wallace, RJ (B22) 2019; 63 DeJesus, MA, Gerrick, ER, Xu, W, Park, SW, Long, JE, Boutte, CC, Rubin, EJ, Schnappinger, D, Ehrt, S, Fortune, SM, Sassetti, CM, Ioerger, TR (B10) 2017; 8 Rodionova, IA, Schuster, BM, Guinn, KM, Sorci, L, Scott, DA, Li, X, Kheterpal, I, Shoen, C, Cynamon, M, Locher, C, Rubin, EJ, Osterman, AL (B91) 2014; 5 Reingewertz, TH, Meyer, T, McIntosh, F, Sullivan, J, Meir, M, Chang, Y-F, Behr, MA, Barkan, D (B77) 2019; 64 Bloom-Ackermann, Z, Navon, S, Gingold, H, Towers, R, Pilpel, Y, Dahan, O (B99) 2014; 10 Lamichhane, G, Zignol, M, Blades, NJ, Geiman, DE, Dougherty, A, Grosset, J, Broman, KW, Bishai, WR (B101) 2003; 100 Kana, BD, Gordhan, BG, Downing, KJ, Sung, N, Vostroktunova, G, Machowski, EE, Tsenova, L, Young, M, Kaprelyants, A, Kaplan, G, Mizrahi, V (B54) 2008; 67 Kim, J-H, O’Brien, KM, Sharma, R, Boshoff, HIM, Rehren, G, Chakraborty, S, Wallach, JB, Monteleone, M, Wilson, DJ, Aldrich, CC, Barry, CE, Rhee, KY, Ehrt, S, Schnappinger, D (B92) 2013; 110 Karzai, AW, Roche, ED, Sauer, RT (B33) 2000; 7 Miranda-CasoLuengo, AA, Staunton, PM, Dinan, AM, Lohan, AJ, Loftus, BJ (B69) 2016; 17 Nixon, MR, Saionz, KW, Koo, M-S, Szymonifka, MJ, Jung, H, Roberts, JP, Nandakumar, M, Kumar, A, Liao, R, Rustad, T, Sacchettini, JC, Rhee, KY, Freundlich, JS, Sherman, DR (B88) 2014; 21 Correale, S, Ruggiero, A, Capparelli, R, Pedone, E, Berisio, R (B56) 2013; 69 Lounis, N, Gevers, T, Van den Berg, J, Vranckx, L, Andries, K (B24) 2009; 53 Hagner, N, Joerger, M (B87) 2010; 2 Merianos, HJ, Wang, J, Moore, PB (B97) 2004; 10 Kieser, KJ, Baranowski, C, Chao, MC, Long, JE, Sassetti, CM, Waldor, MK, Sacchettini, JC, Ioerger, TR, Rubin, EJ (B52) 2015; 112 Vollmer, W, Joris, B, Charlier, P, Foster, S (B94) 2008; 32 Krajewski, WW, Jones, TA, Mowbray, SL (B25) 2005; 102 Zalkin, H, Smith, JL (B65) 1998; 72 Senzani, S, Li, D, Bhaskar, A, Ealand, C, Chang, J, Rimal, B, Liu, C, Joon Kim, S, Dhar, N, Kana, B (B58) 2017; 7 Lopeman, RC, Harrison, J, Desai, M, Cox, JAG (B6) 2019; 7 Nie, WJ, Xie, ZY, Gao, S, Teng, TL, Zhou, WQ, Shang, YY, Jing, W, Shi, WH, Wang, QF, Huang, XR, Cai, BY, Wang, J, Wang, J, Guo, R, Ge, QP, Nie, LH, Han, XQ, Du, YD, Chu, NH (B38) 2020; 33 Jaén-Luchoro, D, Salvà-Serra, F, Aliaga-Lozano, F, Seguí, C, Busquets, A, Ramírez, A, Ruíz, M, Gomila, M, Lalucat, J, Bennasar-Figueras, A (B68) 2016; 4 Holas, O, Ondrejcek, P, Dolezal, M (B44) 2015; 30 Tullius, MV, Harth, G, Horwitz, MA (B84) 2003; 71 Rominski, A, Roditscheff, A, Selchow, P, Bottger, EC, Sander, P (B19) 2017; 72 de Ruyck, J, Dupont, C, Lamy, E, Le Moigne, V, Biot, C, Guérardel, Y, Herrmann, J-L, Blaise, M, Grassin-Delyle, S, Kremer, L, Dubar, F (B82) 2020; 9 Bretl, DJ, Bigley, TM, Terhune, SS, Zahrt, TC (B28) 2014; 196 Zheng, J, Rubin, EJ, Bifani, P, Mathys, V, Lim, V, Au, M, Jang, J, Nam, J, Dick, T, Walker, JR, Pethe, K, Camacho, LR (B90) 2013; 288 Alexander, DC, Vasireddy, R, Vasireddy, S, Philley, JV, Brown-Elliott, BA, Perry, BJ, Griffith, DE, Benwill, JL, Cameron, ADS, Wallace, RJ (B23) 2017; 55 Visentin, M, Zhao, R, Goldman, ID (B86) 2012; 26 Gupta, R, Lavollay, M, Mainardi, JL, Arthur, M, Bishai, WR, Lamichhane, G (B57) 2010; 16 Gutierrez, AV, Richard, M, Roquet-Baneres, F, Viljoen, A, Kremer, L (B78) 2019; 63 Brown-Elliott, BA, Rubio, A, Wallace, RJ (B41) 2018; 62 Personne, Y, Parish, T (B32) 2014; 94 Wang, X, Ahn, Y-M, Lentscher, AG, Lister, JS, Brothers, RC, Kneen, MM, Gerratana, B, Boshoff, HI, Dowd, CS (B93) 2017; 27 Mayer, BK, Falkinham, JO (B30) 1986; 53 Laencina, L, Dubois, V, Le Moigne, V, Viljoen, A, Majlessi, L, Pritchard, J, Bernut, A, Piel, L, Roux, A-L, Gaillard, J-L, Lombard, B, Loew, D, Rubin, EJ, Brosch, R, Kremer, L, Herrmann, J-L, Girard-Misguich, F (B36) 2018; 115 e_1_3_3_96_2 e_1_3_3_50_2 e_1_3_3_77_2 e_1_3_3_16_2 e_1_3_3_39_2 e_1_3_3_12_2 e_1_3_3_58_2 e_1_3_3_35_2 e_1_3_3_92_2 e_1_3_3_54_2 e_1_3_3_31_2 e_1_3_3_73_2 e_1_3_3_61_2 e_1_3_3_88_2 e_1_3_3_5_2 e_1_3_3_105_2 e_1_3_3_9_2 e_1_3_3_27_2 e_1_3_3_23_2 e_1_3_3_69_2 e_1_3_3_46_2 e_1_3_3_80_2 e_1_3_3_65_2 e_1_3_3_42_2 e_1_3_3_84_2 e_1_3_3_101_2 e_1_3_3_76_2 e_1_3_3_99_2 e_1_3_3_38_2 e_1_3_3_15_2 e_1_3_3_34_2 e_1_3_3_57_2 e_1_3_3_91_2 e_1_3_3_11_2 e_1_3_3_30_2 e_1_3_3_53_2 e_1_3_3_72_2 e_1_3_3_95_2 e_1_3_3_60_2 e_1_3_3_87_2 e_1_3_3_8_2 e_1_3_3_104_2 e_1_3_3_49_2 e_1_3_3_26_2 e_1_3_3_45_2 e_1_3_3_68_2 e_1_3_3_4_2 e_1_3_3_22_2 e_1_3_3_41_2 e_1_3_3_64_2 e_1_3_3_83_2 e_1_3_3_100_2 e_1_3_3_75_2 e_1_3_3_71_2 e_1_3_3_98_2 e_1_3_3_79_2 e_1_3_3_18_2 e_1_3_3_37_2 e_1_3_3_90_2 e_1_3_3_14_2 e_1_3_3_56_2 e_1_3_3_33_2 e_1_3_3_94_2 e_1_3_3_10_2 e_1_3_3_52_2 e_1_3_3_40_2 e_1_3_3_86_2 e_1_3_3_7_2 e_1_3_3_29_2 e_1_3_3_48_2 e_1_3_3_25_2 e_1_3_3_67_2 e_1_3_3_44_2 e_1_3_3_82_2 e_1_3_3_103_2 e_1_3_3_3_2 e_1_3_3_21_2 e_1_3_3_63_2 e_1_3_3_51_2 e_1_3_3_74_2 e_1_3_3_97_2 e_1_3_3_70_2 e_1_3_3_78_2 e_1_3_3_17_2 e_1_3_3_13_2 Sha W (e_1_3_3_19_2) 2003; 26 e_1_3_3_36_2 e_1_3_3_59_2 e_1_3_3_32_2 e_1_3_3_55_2 e_1_3_3_93_2 e_1_3_3_62_2 e_1_3_3_85_2 e_1_3_3_89_2 e_1_3_3_6_2 e_1_3_3_106_2 e_1_3_3_28_2 e_1_3_3_24_2 e_1_3_3_47_2 e_1_3_3_2_2 e_1_3_3_20_2 e_1_3_3_43_2 e_1_3_3_66_2 e_1_3_3_81_2 e_1_3_3_102_2 |
References_xml | – volume: 4 year: 2016 ident: B68 article-title: Complete genome sequence of Mycobacterium chelonae type strain CCUG 47445, a rapidly growing species of nontuberculous mycobacteria publication-title: Genome Announc doi: 10.1128/genomeA.00550-16 contributor: fullname: Bennasar-Figueras, A – volume: 154 start-page: 240 year: 2008 end-page: 248 ident: B43 article-title: EmbA is an essential arabinosyltransferase in Mycobacterium tuberculosis publication-title: Microbiology (Reading) doi: 10.1099/mic.0.2007/012153-0 contributor: fullname: Parish, T – volume: 72 start-page: 87 year: 1998 end-page: 144 ident: B65 article-title: Enzymes utilizing glutamine as an amide donor publication-title: Adv Enzymol Relat Areas Mol Biol doi: 10.1002/9780470123188.ch4 contributor: fullname: Smith, JL – volume: 59 start-page: 1455 year: 2015 end-page: 1465 ident: B40 article-title: A novel inhibitor of gyrase B is a potent drug candidate for treatment of tuberculosis and nontuberculosis mycobacterial infections publication-title: Antimicrob Agents Chemother doi: 10.1128/AAC.04347-14 contributor: fullname: Thomson, JA – volume: 8 start-page: 387 year: 2016 end-page: 402 ident: B35 article-title: Mycobacterial pan-genome analysis suggests important role of plasmids in the radiation of type VII secretion systems publication-title: Genome Biol Evol doi: 10.1093/gbe/evw001 contributor: fullname: Sapriel, G – volume: 22 start-page: 510 year: 2017 end-page: 518 ident: B37 article-title: DNA topoisomerase I and DNA gyrase as targets for TB therapy publication-title: Drug Discov Today doi: 10.1016/j.drudis.2016.11.006 contributor: fullname: Maxwell, A – volume: 9 start-page: 351 year: 2020 end-page: 365 ident: B82 article-title: Structure-based design and synthesis of piperidinol-containing molecules as new Mycobacterium abscessus inhibitors publication-title: ChemistryOpen doi: 10.1002/open.202000042 contributor: fullname: Dubar, F – volume: 174 start-page: 1213 year: 1992 end-page: 1221 ident: B98 article-title: Mutagenesis of ribosomal protein S8 from Escherichia coli: defects in regulation of the spc operon publication-title: J Bacteriol doi: 10.1128/jb.174.4.1213-1221.1992 contributor: fullname: Zimmermann, RA – volume: 67 start-page: 672 year: 2008 end-page: 684 ident: B54 article-title: The resuscitation-promoting factors of Mycobacterium tuberculosis are required for virulence and resuscitation from dormancy but are collectively dispensable for growth in vitro publication-title: Mol Microbiol doi: 10.1111/j.1365-2958.2007.06078.x contributor: fullname: Mizrahi, V – volume: 1279 start-page: 79 year: 2015 end-page: 95 ident: B102 article-title: Identifying essential genes in Mycobacterium tuberculosis by global phenotypic profiling publication-title: Methods Mol Biol doi: 10.1007/978-1-4939-2398-4_6 contributor: fullname: Sassetti, CM – volume: 19 start-page: 188 year: 2019 end-page: 191 ident: B60 article-title: Detection and molecular characterization of amikacin-resistant Mycobacterium abscessus isolated from patients with pulmonary disease publication-title: J Glob Antimicrob Resist doi: 10.1016/j.jgar.2019.05.016 contributor: fullname: Chu, H – volume: 112 start-page: 4110 year: 2015 end-page: 4115 ident: B85 article-title: Essential genome of Pseudomonas aeruginosa in cystic fibrosis sputum publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.1419677112 contributor: fullname: Whiteley, M – volume: 47 start-page: W52 year: 2019 end-page: W58 ident: B104 article-title: OrthoVenn2: a web server for whole-genome comparison and annotation of orthologous clusters across multiple species publication-title: Nucleic Acids Res doi: 10.1093/nar/gkz333 contributor: fullname: Wang, Y – volume: 6 year: 2011 ident: B7 article-title: Conditional gene expression in Mycobacterium abscessus publication-title: PLoS One doi: 10.1371/journal.pone.0029306 contributor: fullname: Herrmann, JL – volume: 57 start-page: 155 year: 2003 end-page: 176 ident: B26 article-title: Nitrogen assimilation and global regulation in Escherichia coli publication-title: Annu Rev Microbiol doi: 10.1146/annurev.micro.57.030502.090820 contributor: fullname: Reitzer, L – volume: 2 start-page: 293 year: 2010 end-page: 301 ident: B87 article-title: Cancer chemotherapy: targeting folic acid synthesis publication-title: Cancer Manag Res doi: 10.2147/CMR.S10043 contributor: fullname: Joerger, M – volume: 11 year: 2015 ident: B15 article-title: TRANSIT: a software tool for Himar1 TnSeq analysis publication-title: PLoS Comput Biol doi: 10.1371/journal.pcbi.1004401 contributor: fullname: Ioerger, TR – volume: 18 start-page: 392 year: 2020 end-page: 407 ident: B2 article-title: Non-tuberculous mycobacteria and the rise of Mycobacterium abscessus publication-title: Nat Rev Microbiol doi: 10.1038/s41579-020-0331-1 contributor: fullname: Kremer, L – volume: 10 start-page: 954 year: 2004 end-page: 964 ident: B97 article-title: The structure of a ribosomal protein S8/spc operon mRNA complex publication-title: RNA doi: 10.1261/rna.7030704 contributor: fullname: Moore, PB – volume: 72 start-page: 376 year: 2017 end-page: 384 ident: B19 article-title: Intrinsic rifamycin resistance of Mycobacterium abscessus is mediated by ADP-ribosyltransferase MAB_0591 publication-title: J Antimicrob Chemother doi: 10.1093/jac/dkw466 contributor: fullname: Sander, P – volume: 56 start-page: 4331 year: 2012 end-page: 4340 ident: B17 article-title: Dose-ranging comparison of rifampin and rifapentine in two pathologically distinct murine models of tuberculosis publication-title: Antimicrob Agents Chemother doi: 10.1128/AAC.00912-12 contributor: fullname: Nuermberger, EL – volume: 101 start-page: 515 year: 2016 end-page: 529 ident: B46 article-title: A new piperidinol derivative targeting mycolic acid transport in Mycobacterium abscessus publication-title: Mol Microbiol doi: 10.1111/mmi.13406 contributor: fullname: Kremer, L – volume: 63 year: 2019 ident: B78 article-title: The TetR family transcription factor MAB_2299c regulates the expression of two distinct MmpS-MmpL efflux pumps involved in cross-resistance to clofazimine and bedaquiline in Mycobacterium abscessus publication-title: Antimicrob Agents Chemother doi: 10.1128/AAC.01000-19 contributor: fullname: Kremer, L – volume: 15 start-page: 716 year: 2002 end-page: 746 ident: B1 article-title: Clinical and taxonomic status of pathogenic nonpigmented or late-pigmenting rapidly growing mycobacteria publication-title: Clin Microbiol Rev doi: 10.1128/cmr.15.4.716-746.2002 contributor: fullname: Wallace, RJ – volume: 94 start-page: 34 year: 2014 end-page: 42 ident: B32 article-title: Mycobacterium tuberculosis possesses an unusual tmRNA rescue system publication-title: Tuberculosis (Edinb) doi: 10.1016/j.tube.2013.09.007 contributor: fullname: Parish, T – volume: 9 start-page: 649 year: 2018 ident: B62 article-title: Mechanistic and structural insights into the unique TetR-dependent regulation of a drug efflux pump in Mycobacterium abscessus publication-title: Front Microbiol doi: 10.3389/fmicb.2018.00649 contributor: fullname: Kremer, L – volume: 10 start-page: 1524 year: 2019 ident: B70 article-title: Insights from the genome sequence of Mycobacterium paragordonae, a potential novel live vaccine for preventing mycobacterial infections: the putative role of type VII secretion systems for an intracellular lifestyle within free-living environmental predators publication-title: Front Microbiol doi: 10.3389/fmicb.2019.01524 contributor: fullname: Kim, B-J – volume: 112 start-page: 13087 year: 2015 end-page: 13092 ident: B52 article-title: Peptidoglycan synthesis in Mycobacterium tuberculosis is organized into networks with varying drug susceptibility publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.1514135112 contributor: fullname: Rubin, EJ – volume: 55 start-page: 1107 year: 2016 end-page: 1119 ident: B89 article-title: Structural insights into Mycobacterium tuberculosis Rv2671 protein as a dihydrofolate reductase functional analogue contributing to para-aminosalicylic acid resistance publication-title: Biochemistry doi: 10.1021/acs.biochem.5b00993 contributor: fullname: Sacchettini, JC – volume: 74 start-page: 6491 year: 2006 end-page: 6495 ident: B83 article-title: Protection elicited by two glutamine auxotrophs of Mycobacterium tuberculosis and in vivo growth phenotypes of the four unique glutamine synthetase mutants in a murine model publication-title: Infect Immun doi: 10.1128/IAI.00531-06 contributor: fullname: Jacobs, WR – volume: 28 start-page: 1057 year: 2011 end-page: 1074 ident: B96 article-title: Networks of gene sharing among 329 proteobacterial genomes reveal differences in lateral gene transfer frequency at different phylogenetic depths publication-title: Mol Biol Evol doi: 10.1093/molbev/msq297 contributor: fullname: Dagan, T – volume: 115 start-page: 964 year: 2005 end-page: 965 ident: B3 article-title: Outbreak of atypical mycobacteria infections in U.S. patients traveling abroad for cosmetic surgery publication-title: Plast Reconstr Surg doi: 10.1097/01.prs.0000153818.99552.cc contributor: fullname: Ascherman, JA – volume: 10 start-page: 1 year: 1997 end-page: 18 ident: B29 article-title: Role of oxidants in microbial pathophysiology publication-title: Clin Microbiol Rev doi: 10.1128/CMR.10.1.1-18.1997 contributor: fullname: Britigan, BE – volume: 43 start-page: 181 year: 1999 end-page: 184 ident: B76 article-title: ADP-ribosylation as an intermediate step in inactivation of rifampin by a mycobacterial gene publication-title: Antimicrob Agents Chemother doi: 10.1128/AAC.43.1.181 contributor: fullname: Furihata, K – volume: 21 start-page: 819 year: 2014 end-page: 830 ident: B88 article-title: Folate pathway disruption leads to critical disruption of methionine derivatives in Mycobacterium tuberculosis publication-title: Chem Biol doi: 10.1016/j.chembiol.2014.04.009 contributor: fullname: Sherman, DR – volume: 102 start-page: 14332 year: 2005 end-page: 14337 ident: B95 article-title: Highways of gene sharing in prokaryotes publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.0504068102 contributor: fullname: Ragan, MA – volume: 19 start-page: 5 year: 2017 end-page: 17 ident: B100 article-title: Mycobacterium abscessus ESX-3 plays an important role in host inflammatory and pathological responses during infection publication-title: Microbes Infect doi: 10.1016/j.micinf.2016.09.001 contributor: fullname: Jang, J-C – volume: 63 year: 2019 ident: B22 article-title: Jr In vitro susceptibility testing of bedaquiline against Mycobacterium abscessus complex publication-title: Antimicrob Agents Chemother doi: 10.1128/AAC.01919-18 contributor: fullname: Wallace, RJ – volume: 4 year: 2019 ident: B12 article-title: Global assessment of Mycobacterium avium subsp. hominissuis genetic requirement for growth and virulence publication-title: mSystems doi: 10.1128/mSystems.00402-19 contributor: fullname: Flo, TH – volume: 9 start-page: 4603 year: 2019 ident: B67 article-title: Extended insight into the Mycobacterium chelonae-abscessus complex through whole-genome sequencing of Mycobacterium salmoniphilum outbreak and Mycobacterium salmoniphilum-like strains publication-title: Sci Rep doi: 10.1038/s41598-019-40922-x contributor: fullname: Kirsebom, LA – volume: 33 start-page: 350 year: 2020 end-page: 358 ident: B38 article-title: Efficacy of moxifloxacin against Mycobacterium abscessus in zebrafish model in vivo publication-title: Biomed Environ Sci doi: 10.3967/bes2020.047 contributor: fullname: Chu, NH – volume: 56 start-page: 3549 year: 2012 end-page: 3555 ident: B39 article-title: Activities of moxifloxacin in combination with macrolides against clinical isolates of Mycobacterium abscessus and Mycobacterium massiliense publication-title: Antimicrob Agents Chemother doi: 10.1128/AAC.00685-12 contributor: fullname: Koh, WJ – volume: 71 start-page: 3927 year: 2003 end-page: 3936 ident: B84 article-title: Glutamine synthetase GlnA1 is essential for growth of Mycobacterium tuberculosis in human THP-1 macrophages and guinea pigs publication-title: Infect Immun doi: 10.1128/iai.71.7.3927-3936.2003 contributor: fullname: Horwitz, MA – volume: 62 start-page: 1655 year: 2006 end-page: 1673 ident: B51 article-title: Interaction between FtsW and penicillin-binding protein 3 (PBP3) directs PBP3 to mid-cell, controls cell septation and mediates the formation of a trimeric complex involving FtsZ, FtsW and PBP3 in mycobacteria publication-title: Mol Microbiol doi: 10.1111/j.1365-2958.2006.05491.x contributor: fullname: Basu, J – volume: 27 start-page: 4426 year: 2017 end-page: 4430 ident: B93 article-title: Design, synthesis, and evaluation of substituted nicotinamide adenine dinucleotide (NAD+) synthetase inhibitors as potential antitubercular agents publication-title: Bioorg Med Chem Lett doi: 10.1016/j.bmcl.2017.08.012 contributor: fullname: Dowd, CS – volume: 7 start-page: 90 year: 2019 ident: B6 article-title: Mycobacterium abscessus: environmental bacterium turned clinical nightmare publication-title: Microorganisms doi: 10.3390/microorganisms7030090 contributor: fullname: Cox, JAG – volume: 5 year: 2014 ident: B91 article-title: Metabolic and bactericidal effects of targeted suppression of NadD and NadE enzymes in mycobacteria publication-title: mBio doi: 10.1128/mBio.00747-13 contributor: fullname: Osterman, AL – volume: 110 start-page: 19095 year: 2013 end-page: 19100 ident: B92 article-title: A genetic strategy to identify targets for the development of drugs that prevent bacterial persistence publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.1315860110 contributor: fullname: Schnappinger, D – volume: 61 year: 2017 ident: B61 article-title: Antagonism between front-line antibiotics clarithromycin and amikacin in the treatment of Mycobacterium abscessus infections is mediated by the whiB7 gene publication-title: Antimicrob Agents Chemother doi: 10.1128/AAC.01353-17 contributor: fullname: Thompson, CJ – volume: 5 year: 2020 ident: B9 article-title: A simplified and efficient method for Himar-1 transposon sequencing in bacteria, demonstrated by creation and analysis of a saturated transposon-mutant library in Mycobacterium abscessus publication-title: mSystems doi: 10.1128/mSystems.00976-20 contributor: fullname: Barkan, D – volume: 8 start-page: 261 year: 2019 ident: B20 article-title: Re-understanding the mechanisms of action of the anti-mycobacterial drug bedaquiline publication-title: Antibiotics (Basel) doi: 10.3390/antibiotics8040261 contributor: fullname: Dick, T – volume: 288 start-page: 23447 year: 2013 end-page: 23456 ident: B90 article-title: para-Aminosalicylic acid is a prodrug targeting dihydrofolate reductase in Mycobacterium tuberculosis publication-title: J Biol Chem doi: 10.1074/jbc.M113.475798 contributor: fullname: Camacho, LR – volume: 5 year: 2009 ident: B34 article-title: Systematic genetic nomenclature for type VII secretion systems publication-title: PLoS Pathog doi: 10.1371/journal.ppat.1000507 contributor: fullname: Brosch, R – volume: 25 start-page: 3746 year: 2017 end-page: 3755 ident: B79 article-title: Design, synthesis and evaluation of indole-2-carboxamides with pan anti-mycobacterial activity publication-title: Bioorg Med Chem doi: 10.1016/j.bmc.2017.05.015 contributor: fullname: North, EJ – volume: 102 start-page: 10499 year: 2005 end-page: 10504 ident: B25 article-title: Structure of Mycobacterium tuberculosis glutamine synthetase in complex with a transition-state mimic provides functional insights publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.0502248102 contributor: fullname: Mowbray, SL – volume: 175 start-page: 367 year: 2007 end-page: 416 ident: B73 article-title: An official ATS/IDSA statement: diagnosis, treatment, and prevention of nontuberculous mycobacterial diseases publication-title: Am J Respir Crit Care Med doi: 10.1164/rccm.200604-571ST contributor: fullname: Winthrop, K – volume: 27 start-page: 74 year: 2020 ident: B45 article-title: Of tuberculosis and non-tuberculous mycobacterial infections: a comparative analysis of epidemiology, diagnosis and treatment publication-title: J Biomed Sci doi: 10.1186/s12929-020-00667-6 contributor: fullname: Subbian, S – volume: 17 start-page: 553 year: 2016 ident: B69 article-title: Functional characterization of the Mycobacterium abscessus genome coupled with condition specific transcriptomics reveals conserved molecular strategies for host adaptation and persistence publication-title: BMC Genomics doi: 10.1186/s12864-016-2868-y contributor: fullname: Loftus, BJ – volume: 354 start-page: 751 year: 2016 end-page: 757 ident: B4 article-title: Emergence and spread of a human-transmissible multidrug-resistant nontuberculous mycobacterium publication-title: Science doi: 10.1126/science.aaf8156 contributor: fullname: Kidd, TJ – volume: 32 start-page: 259 year: 2008 end-page: 286 ident: B94 article-title: Bacterial peptidoglycan (murein) hydrolases publication-title: FEMS Microbiol Rev doi: 10.1111/j.1574-6976.2007.00099.x contributor: fullname: Foster, S – volume: 156 start-page: 173 year: 2005 end-page: 177 ident: B66 article-title: Glutamine amidotransferase activity of NAD+ synthetase from Mycobacterium tuberculosis depends on an amino-terminal nitrilase domain publication-title: Res Microbiol doi: 10.1016/j.resmic.2004.08.011 contributor: fullname: Riccardi, G – volume: 63 year: 2019 ident: B81 article-title: Indole-2-carboxamides are active against Mycobacterium abscessus in a mouse model of acute infection publication-title: Antimicrob Agents Chemother doi: 10.1128/AAC.02245-18 contributor: fullname: North, EJ – volume: 115 start-page: E1002 year: 2018 end-page: E1011 ident: B36 article-title: Identification of genes required for Mycobacterium abscessus growth in vivo with a prominent role of the ESX-4 locus publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.1713195115 contributor: fullname: Girard-Misguich, F – volume: 15 start-page: 359 year: 2014 ident: B72 article-title: Genome analysis reveals three genomospecies in Mycobacterium abscessus publication-title: BMC Genomics doi: 10.1186/1471-2164-15-359 contributor: fullname: Drancourt, M – volume: 116 start-page: 19646 year: 2019 end-page: 19651 ident: B27 article-title: Mode-of-action profiling reveals glutamine synthetase as a collateral metabolic vulnerability of Mycobacterium tuberculosis to bedaquiline publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.1907946116 contributor: fullname: Rhee, KY – volume: 8 year: 2017 ident: B10 article-title: Comprehensive essentiality analysis of the Mycobacterium tuberculosis genome via saturating transposon mutagenesis publication-title: mBio doi: 10.1128/mBio.02133-16 contributor: fullname: Ioerger, TR – volume: 26 start-page: 544 year: 2003 end-page: 547 ident: B18 article-title: Investigation of drug-resistance to rifampin and rpoB gene sequence analysis of Mycobacterium abscessus publication-title: Chin J Tuberc Respir Dis contributor: fullname: He, GJ – volume: 14 start-page: 75 year: 2014 ident: B49 article-title: Comparative genomics for mycobacterial peptidoglycan remodelling enzymes reveals extensive genetic multiplicity publication-title: BMC Microbiol doi: 10.1186/1471-2180-14-75 contributor: fullname: Kana, BD – volume: 64 year: 2019 ident: B77 article-title: Differential sensitivity of mycobacteria to isoniazid is related to differences in KatG-mediated enzymatic activation of the drug publication-title: Antimicrob Agents Chemother doi: 10.1128/AAC.01899-19 contributor: fullname: Barkan, D – volume: 75 start-page: 1331 year: 2009 end-page: 1338 ident: B8 article-title: Construction of Mycobacterium abscessus defined glycopeptidolipid mutants: comparison of genetic tools publication-title: Appl Environ Microbiol doi: 10.1128/AEM.01914-08 contributor: fullname: Reyrat, JM – ident: B74 article-title: Hasan NA , Davidson RM , Epperson LE , Kammlade SM , Rodger RR , Levin AR . 2019 . Population genomics of nontuberculous mycobacteria recovered from United States cystic fibrosis patients . bioRxiv 663559 . doi: 10.1101/663559 . – volume: 53 start-page: 4927 year: 2009 end-page: 4929 ident: B24 article-title: ATP synthase inhibition of Mycobacterium avium is not bactericidal publication-title: Antimicrob Agents Chemother doi: 10.1128/AAC.00689-09 contributor: fullname: Andries, K – volume: 10 start-page: 13 year: 2020 end-page: 22 ident: B71 article-title: Comparative analysis of whole-genome and methylome profiles of a smooth and a rough Mycobacterium abscessus clinical strain publication-title: G3 (Bethesda) doi: 10.1534/g3.119.400737 contributor: fullname: Zhang, T – volume: 200 year: 2018 ident: B53 article-title: Two dd-carboxypeptidases from Mycobacterium smegmatis affect cell surface properties through regulation of peptidoglycan cross-linking and glycopeptidolipids publication-title: J Bacteriol doi: 10.1128/JB.00760-17 contributor: fullname: Ghosh, AS – volume: 16 start-page: 466 year: 2010 end-page: 469 ident: B57 article-title: The Mycobacterium tuberculosis protein LdtMt2 is a nonclassical transpeptidase required for virulence and resistance to amoxicillin publication-title: Nat Med doi: 10.1038/nm.2120 contributor: fullname: Lamichhane, G – volume: 10 start-page: 1095 year: 2020 ident: B11 article-title: Identifying the essential genes of Mycobacterium avium subsp. hominissuis with Tn-Seq using a rank-based filter procedure publication-title: Sci Rep doi: 10.1038/s41598-020-57845-7 contributor: fullname: Karakousis, PC – volume: 293 start-page: 6497 year: 2018 end-page: 6516 ident: B50 article-title: The transpeptidase PbpA and noncanonical transglycosylase RodA of Mycobacterium tuberculosis play important roles in regulating bacterial cell lengths publication-title: J Biol Chem doi: 10.1074/jbc.M117.811190 contributor: fullname: Nandicoori, VK – volume: 8 start-page: 11 year: 2011 end-page: 13 ident: B105 article-title: ARNold: a web tool for the prediction of Rho-independent transcription terminators publication-title: RNA Biol doi: 10.4161/rna.8.1.13346 contributor: fullname: Gautheret, D – volume: 30 start-page: 629 year: 2015 end-page: 648 ident: B44 article-title: Mycobacterium tuberculosis enoyl-acyl carrier protein reductase inhibitors as potential antituberculotics: development in the past decade publication-title: J Enzyme Inhib Med Chem J doi: 10.3109/14756366.2014.959512 contributor: fullname: Dolezal, M – volume: 4 year: 2009 ident: B14 article-title: Non mycobacterial virulence genes in the genome of the emerging pathogen Mycobacterium abscessus publication-title: PLoS One doi: 10.1371/journal.pone.0005660 contributor: fullname: Gaillard, J-L – volume: 14 start-page: 303 year: 2013 ident: B16 article-title: A Hidden Markov Model for identifying essential and growth-defect regions in bacterial genomes from transposon insertion sequencing data publication-title: BMC Bioinformatics doi: 10.1186/1471-2105-14-303 contributor: fullname: Ioerger, TR – volume: 55 start-page: 574 year: 2017 end-page: 584 ident: B23 article-title: Emergence of mmpT5 variants during bedaquiline treatment of Mycobacterium intracellulare lung disease publication-title: J Clin Microbiol doi: 10.1128/JCM.02087-16 contributor: fullname: Wallace, RJ – volume: 20 year: 2019 ident: B5 article-title: Mycobacterium abscessus, an emerging and worrisome pathogen among cystic fibrosis patients publication-title: Int J Mol Sci doi: 10.3390/ijms20235868 contributor: fullname: Pasca, MR – volume: 62 year: 2018 ident: B41 article-title: In vitro susceptibility testing of a novel benzimidazole, SPR719, against nontuberculous mycobacteria publication-title: Antimicrob Agents Chemother doi: 10.1128/AAC.01503-18 contributor: fullname: Wallace, RJ – volume: 4 year: 2019 ident: B13 article-title: Genomewide assessment of Mycobacterium tuberculosis conditionally essential metabolic pathways publication-title: mSystems doi: 10.1128/mSystems.00070-19 contributor: fullname: Baughn, AD – volume: 61 year: 2017 ident: B21 article-title: Bedaquiline inhibits the ATP synthase in Mycobacterium abscessus and is effective in infected zebrafish publication-title: Antimicrob Agents Chemother doi: 10.1128/AAC.01225-17 contributor: fullname: Kremer, L – volume: 196 start-page: 391 year: 2014 end-page: 406 ident: B28 article-title: The MprB extracytoplasmic domain negatively regulates activation of the Mycobacterium tuberculosis MprAB two-component system publication-title: J Bacteriol doi: 10.1128/JB.01064-13 contributor: fullname: Zahrt, TC – volume: 26 start-page: 629 year: 2012 end-page: 648 ident: B86 article-title: The antifolates publication-title: Hematol Oncol Clin North Am doi: 10.1016/j.hoc.2012.02.002 contributor: fullname: Goldman, ID – volume: 100 start-page: 7213 year: 2003 end-page: 7218 ident: B101 article-title: A postgenomic method for predicting essential genes at subsaturation levels of mutagenesis: application to Mycobacterium tuberculosis publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.1231432100 contributor: fullname: Bishai, WR – volume: 7 start-page: 449 year: 2000 end-page: 455 ident: B33 article-title: The SsrA-SmpB system for protein tagging, directed degradation and ribosome rescue publication-title: Nat Struct Biol doi: 10.1038/75843 contributor: fullname: Sauer, RT – volume: 12 start-page: 709 year: 2002 end-page: 720 ident: B64 article-title: Structural biology of enzymes involved in NAD and molybdenum cofactor biosynthesis publication-title: Curr Opin Struct Biol doi: 10.1016/S0959-440X(02)00385-8 contributor: fullname: Schindelin, H – volume: 10 year: 2014 ident: B99 article-title: A comprehensive tRNA deletion library unravels the genetic architecture of the tRNA pool publication-title: PLoS Genet doi: 10.1371/journal.pgen.1004084 contributor: fullname: Dahan, O – volume: 53 start-page: 1367 year: 2009 end-page: 1376 ident: B75 article-title: A novel gene, erm(41), confers inducible macrolide resistance to clinical isolates of Mycobacterium abscessus but is absent from Mycobacterium chelonae publication-title: Antimicrob Agents Chemother doi: 10.1128/AAC.01275-08 contributor: fullname: Wallace, RJ – volume: 7 start-page: 1140 year: 2017 ident: B58 article-title: An amidase_3 domain-containing N-acetylmuramyl-l-alanine amidase is required for mycobacterial cell division publication-title: Sci Rep doi: 10.1038/s41598-017-01184-7 contributor: fullname: Kana, B – volume: 53 start-page: 631 year: 1986 end-page: 635 ident: B30 article-title: Superoxide dismutase activity of Mycobacterium avium, M. intracellulare, and M. scrofulaceum publication-title: Infect Immun doi: 10.1128/IAI.53.3.631-635.1986 contributor: fullname: Falkinham, JO – volume: 35 start-page: 1325 year: 2007 end-page: 1328 ident: B48 article-title: Structure, function and biosynthesis of the Mycobacterium tuberculosis cell wall: arabinogalactan and lipoarabinomannan assembly with a view to discovering new drug targets publication-title: Biochem Soc Trans doi: 10.1042/BST0351325 contributor: fullname: Besra, GS – volume: 69 start-page: 1697 year: 2013 end-page: 1706 ident: B56 article-title: Structures of free and inhibited forms of the l,d-transpeptidase LdtMt1 from Mycobacterium tuberculosis publication-title: Acta Crystallogr D Biol Crystallogr doi: 10.1107/S0907444913013085 contributor: fullname: Berisio, R – volume: 61 year: 2017 ident: B55 article-title: Mycobacterium abscessus l,d-transpeptidases are susceptible to inactivation by carbapenems and cephalosporins but not penicillins publication-title: Antimicrob Agents Chemother doi: 10.1128/AAC.00866-17 contributor: fullname: Lamichhane, G – volume: 6 start-page: 1323 year: 2020 end-page: 1331 ident: B42 article-title: Advancement of GyrB inhibitors for treatment of infections caused by Mycobacterium tuberculosis and non-tuberculous mycobacteria publication-title: ACS Infect Dis doi: 10.1021/acsinfecdis.0c00025 contributor: fullname: Pucci, MJ – volume: 66 start-page: 480 year: 2013 end-page: 488 ident: B31 article-title: The role of superoxide dismutase in the survival of Mycobacterium tuberculosis in macrophages publication-title: Jpn J Infect Dis doi: 10.7883/yoken.66.480 contributor: fullname: Bao, L – volume: 60 start-page: 5876 year: 2017 end-page: 5888 ident: B80 article-title: Targeting mycolic acid transport by indole-2-carboxamides for the treatment of Mycobacterium abscessus infections publication-title: J Med Chem doi: 10.1021/acs.jmedchem.7b00582 contributor: fullname: Kremer, L – volume: 69 start-page: 691 year: 2014 end-page: 696 ident: B47 article-title: Characterization of broad-spectrum Mycobacterium abscessus class A beta-lactamase publication-title: J Antimicrob Chemother doi: 10.1093/jac/dkt410 contributor: fullname: Arthur, M – volume: 69 start-page: 2543 year: 2013 end-page: 2554 ident: B59 article-title: The structure of Rv3717 reveals a novel amidase from Mycobacterium tuberculosis publication-title: Acta Crystallogr D Biol Crystallogr doi: 10.1107/S0907444913026371 contributor: fullname: Taneja, B – volume: 293 start-page: 7397 year: 2018 end-page: 7407 ident: B63 article-title: Kinetics and structural features of dimeric glutamine-dependent bacterial NAD+ synthetases suggest evolutionary adaptation to available metabolites publication-title: J Biol Chem doi: 10.1074/jbc.RA118.002241 contributor: fullname: Huergo, LF – volume: 30 start-page: 2114 year: 2014 end-page: 2120 ident: B103 article-title: Trimmomatic: a flexible trimmer for Illumina sequence data publication-title: Bioinformatics doi: 10.1093/bioinformatics/btu170 contributor: fullname: Usadel, B – ident: e_1_3_3_70_2 doi: 10.1186/s12864-016-2868-y – ident: e_1_3_3_56_2 doi: 10.1128/AAC.00866-17 – ident: e_1_3_3_49_2 doi: 10.1042/BST0351325 – ident: e_1_3_3_81_2 doi: 10.1021/acs.jmedchem.7b00582 – ident: e_1_3_3_76_2 doi: 10.1128/AAC.01275-08 – ident: e_1_3_3_94_2 doi: 10.1016/j.bmcl.2017.08.012 – ident: e_1_3_3_93_2 doi: 10.1073/pnas.1315860110 – ident: e_1_3_3_78_2 doi: 10.1128/AAC.01899-19 – ident: e_1_3_3_97_2 doi: 10.1093/molbev/msq297 – ident: e_1_3_3_79_2 doi: 10.1128/AAC.01000-19 – ident: e_1_3_3_15_2 doi: 10.1371/journal.pone.0005660 – ident: e_1_3_3_98_2 doi: 10.1261/rna.7030704 – ident: e_1_3_3_64_2 doi: 10.1074/jbc.RA118.002241 – volume: 26 start-page: 544 year: 2003 ident: e_1_3_3_19_2 article-title: Investigation of drug-resistance to rifampin and rpoB gene sequence analysis of Mycobacterium abscessus publication-title: Chin J Tuberc Respir Dis contributor: fullname: Sha W – ident: e_1_3_3_14_2 doi: 10.1128/mSystems.00070-19 – ident: e_1_3_3_50_2 doi: 10.1186/1471-2180-14-75 – ident: e_1_3_3_100_2 doi: 10.1371/journal.pgen.1004084 – ident: e_1_3_3_72_2 doi: 10.1534/g3.119.400737 – ident: e_1_3_3_8_2 doi: 10.1371/journal.pone.0029306 – ident: e_1_3_3_34_2 doi: 10.1038/75843 – ident: e_1_3_3_20_2 doi: 10.1093/jac/dkw466 – ident: e_1_3_3_27_2 doi: 10.1146/annurev.micro.57.030502.090820 – ident: e_1_3_3_37_2 doi: 10.1073/pnas.1713195115 – ident: e_1_3_3_65_2 doi: 10.1016/S0959-440X(02)00385-8 – ident: e_1_3_3_83_2 doi: 10.1002/open.202000042 – ident: e_1_3_3_48_2 doi: 10.1093/jac/dkt410 – ident: e_1_3_3_96_2 doi: 10.1073/pnas.0504068102 – ident: e_1_3_3_85_2 doi: 10.1128/iai.71.7.3927-3936.2003 – ident: e_1_3_3_25_2 doi: 10.1128/AAC.00689-09 – ident: e_1_3_3_71_2 doi: 10.3389/fmicb.2019.01524 – ident: e_1_3_3_80_2 doi: 10.1016/j.bmc.2017.05.015 – ident: e_1_3_3_57_2 doi: 10.1107/S0907444913013085 – ident: e_1_3_3_61_2 doi: 10.1016/j.jgar.2019.05.016 – ident: e_1_3_3_21_2 doi: 10.3390/antibiotics8040261 – ident: e_1_3_3_42_2 doi: 10.1128/AAC.01503-18 – ident: e_1_3_3_51_2 doi: 10.1074/jbc.M117.811190 – ident: e_1_3_3_12_2 doi: 10.1038/s41598-020-57845-7 – ident: e_1_3_3_41_2 doi: 10.1128/AAC.04347-14 – ident: e_1_3_3_46_2 doi: 10.1186/s12929-020-00667-6 – ident: e_1_3_3_82_2 doi: 10.1128/AAC.02245-18 – ident: e_1_3_3_104_2 doi: 10.1093/bioinformatics/btu170 – ident: e_1_3_3_91_2 doi: 10.1074/jbc.M113.475798 – ident: e_1_3_3_26_2 doi: 10.1073/pnas.0502248102 – ident: e_1_3_3_63_2 doi: 10.3389/fmicb.2018.00649 – ident: e_1_3_3_69_2 doi: 10.1128/genomeA.00550-16 – ident: e_1_3_3_6_2 doi: 10.3390/ijms20235868 – ident: e_1_3_3_17_2 doi: 10.1186/1471-2105-14-303 – ident: e_1_3_3_54_2 doi: 10.1128/JB.00760-17 – ident: e_1_3_3_75_2 doi: 10.1101/663559 – ident: e_1_3_3_58_2 doi: 10.1038/nm.2120 – ident: e_1_3_3_45_2 doi: 10.3109/14756366.2014.959512 – ident: e_1_3_3_84_2 doi: 10.1128/IAI.00531-06 – ident: e_1_3_3_102_2 doi: 10.1073/pnas.1231432100 – ident: e_1_3_3_52_2 doi: 10.1111/j.1365-2958.2006.05491.x – ident: e_1_3_3_101_2 doi: 10.1016/j.micinf.2016.09.001 – ident: e_1_3_3_87_2 doi: 10.1016/j.hoc.2012.02.002 – ident: e_1_3_3_9_2 doi: 10.1128/AEM.01914-08 – ident: e_1_3_3_16_2 doi: 10.1371/journal.pcbi.1004401 – ident: e_1_3_3_88_2 doi: 10.2147/CMR.S10043 – ident: e_1_3_3_13_2 doi: 10.1128/mSystems.00402-19 – ident: e_1_3_3_43_2 doi: 10.1021/acsinfecdis.0c00025 – ident: e_1_3_3_38_2 doi: 10.1016/j.drudis.2016.11.006 – ident: e_1_3_3_24_2 doi: 10.1128/JCM.02087-16 – ident: e_1_3_3_74_2 doi: 10.1164/rccm.200604-571ST – ident: e_1_3_3_29_2 doi: 10.1128/JB.01064-13 – ident: e_1_3_3_39_2 doi: 10.3967/bes2020.047 – ident: e_1_3_3_47_2 doi: 10.1111/mmi.13406 – ident: e_1_3_3_44_2 doi: 10.1099/mic.0.2007/012153-0 – ident: e_1_3_3_95_2 doi: 10.1111/j.1574-6976.2007.00099.x – ident: e_1_3_3_77_2 doi: 10.1128/AAC.43.1.181 – ident: e_1_3_3_86_2 doi: 10.1073/pnas.1419677112 – ident: e_1_3_3_22_2 doi: 10.1128/AAC.01225-17 – ident: e_1_3_3_28_2 doi: 10.1073/pnas.1907946116 – ident: e_1_3_3_103_2 doi: 10.1007/978-1-4939-2398-4_6 – ident: e_1_3_3_53_2 doi: 10.1073/pnas.1514135112 – ident: e_1_3_3_23_2 doi: 10.1128/AAC.01919-18 – ident: e_1_3_3_31_2 doi: 10.1128/IAI.53.3.631-635.1986 – ident: e_1_3_3_55_2 doi: 10.1111/j.1365-2958.2007.06078.x – ident: e_1_3_3_106_2 doi: 10.4161/rna.8.1.13346 – ident: e_1_3_3_89_2 doi: 10.1016/j.chembiol.2014.04.009 – ident: e_1_3_3_32_2 doi: 10.7883/yoken.66.480 – ident: e_1_3_3_7_2 doi: 10.3390/microorganisms7030090 – ident: e_1_3_3_10_2 doi: 10.1128/mSystems.00976-20 – ident: e_1_3_3_105_2 doi: 10.1093/nar/gkz333 – ident: e_1_3_3_36_2 doi: 10.1093/gbe/evw001 – ident: e_1_3_3_66_2 doi: 10.1002/9780470123188.ch4 – ident: e_1_3_3_59_2 doi: 10.1038/s41598-017-01184-7 – ident: e_1_3_3_67_2 doi: 10.1016/j.resmic.2004.08.011 – ident: e_1_3_3_40_2 doi: 10.1128/AAC.00685-12 – ident: e_1_3_3_60_2 doi: 10.1107/S0907444913026371 – ident: e_1_3_3_5_2 doi: 10.1126/science.aaf8156 – ident: e_1_3_3_4_2 doi: 10.1097/01.prs.0000153818.99552.cc – ident: e_1_3_3_73_2 doi: 10.1186/1471-2164-15-359 – ident: e_1_3_3_18_2 doi: 10.1128/AAC.00912-12 – ident: e_1_3_3_35_2 doi: 10.1371/journal.ppat.1000507 – ident: e_1_3_3_30_2 doi: 10.1128/CMR.10.1.1-18.1997 – ident: e_1_3_3_68_2 doi: 10.1038/s41598-019-40922-x – ident: e_1_3_3_92_2 doi: 10.1128/mBio.00747-13 – ident: e_1_3_3_11_2 doi: 10.1128/mBio.02133-16 – ident: e_1_3_3_33_2 doi: 10.1016/j.tube.2013.09.007 – ident: e_1_3_3_90_2 doi: 10.1021/acs.biochem.5b00993 – ident: e_1_3_3_99_2 doi: 10.1128/jb.174.4.1213-1221.1992 – ident: e_1_3_3_62_2 doi: 10.1128/AAC.01353-17 – ident: e_1_3_3_2_2 doi: 10.1128/cmr.15.4.716-746.2002 – ident: e_1_3_3_3_2 doi: 10.1038/s41579-020-0331-1 |
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Snippet | Mycobacterium abscessus is an emerging opportunistic human pathogen that naturally resists most major classes of antibiotics, making infections difficult to... Limited knowledge regarding Mycobacterium abscessus pathogenesis and intrinsic resistance to most classes of antibiotics is a major obstacle to developing more... Mycobacterium abscessus is an emerging opportunistic human pathogen that naturally resists most major classes of antibiotics, making infections difficult to... Limited knowledge regarding Mycobacterium abscessusM. abscessusin vitroM. tuberculosisM. aviumhominissuis |
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SubjectTerms | DNA Transposable Elements Genes, Essential Genome, Bacterial Genomics - methods High-Throughput Nucleotide Sequencing - methods Humans Mutagenesis, Insertional Mycobacterium abscessus - genetics Mycobacterium abscessus - pathogenicity Mycobacterium tuberculosis - genetics Research Article |
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Title | Genome-Wide Essentiality Analysis of Mycobacterium abscessus by Saturated Transposon Mutagenesis and Deep Sequencing |
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