Staphylococcus aureus delta toxin modulates both extracellular membrane vesicle biogenesis and amyloid formation

Extracellular membrane vesicles (MVs) produced by in planktonic cultures encapsulate a diverse cargo of bacterial proteins, nucleic acids, and glycopolymers that are protected from destruction by external factors. δ-toxin, a member of the phenol soluble modulin family, was shown to be critical for M...

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Published inmBio Vol. 14; no. 5; p. e0174823
Main Authors Wang, Xiaogang, Uppu, Divakara Ssm, Dickey, Seth W, Burgin, Dylan J, Otto, Michael, Lee, Jean C
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 31.10.2023
Subjects
Amyloid - metabolism
amyloid fibrils
Animals
Bacterial Proteins - metabolism
Bacteriology
delta-toxin
extracellular membrane vesicles
Mice
phenol-soluble modulins
Research Article
Staphylococcal Infections - microbiology
Staphylococcus aureus
Staphylococcus aureus - metabolism
phenol-soluble modulins
delta-toxin
amyloid fibrils
extracellular membrane vesicles
Staphylococcus aureus
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Abstract Extracellular membrane vesicles (MVs) produced by in planktonic cultures encapsulate a diverse cargo of bacterial proteins, nucleic acids, and glycopolymers that are protected from destruction by external factors. δ-toxin, a member of the phenol soluble modulin family, was shown to be critical for MV biogenesis. Amyloid fibrils co-purified with MVs generated by virulent, community-acquired strains, and fibril formation was dependent on expression of the δ-toxin gene ( ). Mass spectrometry data confirmed that the amyloid fibrils were comprised of δ-toxin. Although MVs were produced in a localized murine infection model, amyloid fibrils were not observed in the setting. Our findings provide critical insights into staphylococcal factors involved in MV biogenesis and amyloid formation.
AbstractList IMPORTANCEExtracellular membrane vesicles (MVs) produced by Staphylococcus aureus in planktonic cultures encapsulate a diverse cargo of bacterial proteins, nucleic acids, and glycopolymers that are protected from destruction by external factors. δ-toxin, a member of the phenol soluble modulin family, was shown to be critical for MV biogenesis. Amyloid fibrils co-purified with MVs generated by virulent, community-acquired S. aureus strains, and fibril formation was dependent on expression of the S. aureus δ-toxin gene (hld). Mass spectrometry data confirmed that the amyloid fibrils were comprised of δ-toxin. Although S. aureus MVs were produced in vivo in a localized murine infection model, amyloid fibrils were not observed in the in vivo setting. Our findings provide critical insights into staphylococcal factors involved in MV biogenesis and amyloid formation.
ABSTRACT Staphylococcus aureus secretes phenol-soluble modulins (PSMs), a family of small, amphipathic, secreted peptides with multiple biologic activities. Community-acquired S. aureus strains produce high levels of PSMs in planktonic cultures, and PSM alpha peptides have been shown to augment the release of extracellular membrane vesicles (MVs). We observed that amyloids, aggregates of proteins characterized by a fibrillar morphology and stained with specific dyes, co-purified with MVs harvested from cell-free culture supernatants of community-acquired S. aureus strains. δ-toxin was a major component of amyloid fibrils that co-purified with strain LAC MVs, and δ-toxin promoted the production of MVs and amyloid fibrils in a dose-dependent manner. To determine whether MVs and amyloid fibrils were generated under in vivo conditions, we inoculated mice with S. aureus harvested from planktonic cultures. Bacterial MVs were isolated and purified from lavage fluids recovered from infected animals. Although δ-toxin was the most abundant PSM in lavage fluids, amyloid fibrils could not be detected in these samples. Our findings expand our understanding of amyloid fibril formation in S. aureus cultures, reveal the important roles of δ-toxin in amyloid fibril formation and MV biogenesis, and demonstrate that MVs are generated in vivo in a staphylococcal infection model. IMPORTANCE Extracellular membrane vesicles (MVs) produced by Staphylococcus aureus in planktonic cultures encapsulate a diverse cargo of bacterial proteins, nucleic acids, and glycopolymers that are protected from destruction by external factors. δ-toxin, a member of the phenol soluble modulin family, was shown to be critical for MV biogenesis. Amyloid fibrils co-purified with MVs generated by virulent, community-acquired S. aureus strains, and fibril formation was dependent on expression of the S. aureus δ-toxin gene (hld). Mass spectrometry data confirmed that the amyloid fibrils were comprised of δ-toxin. Although S. aureus MVs were produced in vivo in a localized murine infection model, amyloid fibrils were not observed in the in vivo setting. Our findings provide critical insights into staphylococcal factors involved in MV biogenesis and amyloid formation.
Staphylococcus aureus secretes phenol-soluble modulins (PSMs), a family of small, amphipathic, secreted peptides with multiple biologic activities. Community-acquired S. aureus strains produce high levels of PSMs in planktonic cultures, and PSM alpha peptides have been shown to augment the release of extracellular membrane vesicles (MVs). We observed that amyloids, aggregates of proteins characterized by a fibrillar morphology and stained with specific dyes, co-purified with MVs harvested from cell-free culture supernatants of community-acquired S. aureus strains. δ-toxin was a major component of amyloid fibrils that co-purified with strain LAC MVs, and δ-toxin promoted the production of MVs and amyloid fibrils in a dose-dependent manner. To determine whether MVs and amyloid fibrils were generated under in vivo conditions, we inoculated mice with S. aureus harvested from planktonic cultures. Bacterial MVs were isolated and purified from lavage fluids recovered from infected animals. Although δ-toxin was the most abundant PSM in lavage fluids, amyloid fibrils could not be detected in these samples. Our findings expand our understanding of amyloid fibril formation in S. aureus cultures, reveal the important roles of δ-toxin in amyloid fibril formation and MV biogenesis, and demonstrate that MVs are generated in vivo in a staphylococcal infection model. IMPORTANCE Extracellular membrane vesicles (MVs) produced by Staphylococcus aureus in planktonic cultures encapsulate a diverse cargo of bacterial proteins, nucleic acids, and glycopolymers that are protected from destruction by external factors. δ-toxin, a member of the phenol soluble modulin family, was shown to be critical for MV biogenesis. Amyloid fibrils co-purified with MVs generated by virulent, community-acquired S. aureus strains, and fibril formation was dependent on expression of the S. aureus δ-toxin gene (hld). Mass spectrometry data confirmed that the amyloid fibrils were comprised of δ-toxin. Although S. aureus MVs were produced in vivo in a localized murine infection model, amyloid fibrils were not observed in the in vivo setting. Our findings provide critical insights into staphylococcal factors involved in MV biogenesis and amyloid formation.
ABSTRACT Staphylococcus aureus secretes phenol-soluble modulins (PSMs), a family of small, amphipathic, secreted peptides with multiple biologic activities. Community-acquired S. aureus strains produce high levels of PSMs in planktonic cultures, and PSM alpha peptides have been shown to augment the release of extracellular membrane vesicles (MVs). We observed that amyloids, aggregates of proteins characterized by a fibrillar morphology and stained with specific dyes, co-purified with MVs harvested from cell-free culture supernatants of community-acquired S. aureus strains. δ-toxin was a major component of amyloid fibrils that co-purified with strain LAC MVs, and δ-toxin promoted the production of MVs and amyloid fibrils in a dose-dependent manner. To determine whether MVs and amyloid fibrils were generated under in vivo conditions, we inoculated mice with S. aureus harvested from planktonic cultures. Bacterial MVs were isolated and purified from lavage fluids recovered from infected animals. Although δ-toxin was the most abundant PSM in lavage fluids, amyloid fibrils could not be detected in these samples. Our findings expand our understanding of amyloid fibril formation in S. aureus cultures, reveal the important roles of δ-toxin in amyloid fibril formation and MV biogenesis, and demonstrate that MVs are generated in vivo in a staphylococcal infection model. IMPORTANCE Extracellular membrane vesicles (MVs) produced by Staphylococcus aureus in planktonic cultures encapsulate a diverse cargo of bacterial proteins, nucleic acids, and glycopolymers that are protected from destruction by external factors. δ-toxin, a member of the phenol soluble modulin family, was shown to be critical for MV biogenesis. Amyloid fibrils co-purified with MVs generated by virulent, community-acquired S. aureus strains, and fibril formation was dependent on expression of the S. aureus δ-toxin gene ( hld ). Mass spectrometry data confirmed that the amyloid fibrils were comprised of δ-toxin. Although S. aureus MVs were produced in vivo in a localized murine infection model, amyloid fibrils were not observed in the in vivo setting. Our findings provide critical insights into staphylococcal factors involved in MV biogenesis and amyloid formation. Extracellular membrane vesicles (MVs) produced by Staphylococcus aureus in planktonic cultures encapsulate a diverse cargo of bacterial proteins, nucleic acids, and glycopolymers that are protected from destruction by external factors. δ-toxin, a member of the phenol soluble modulin family, was shown to be critical for MV biogenesis. Amyloid fibrils co-purified with MVs generated by virulent, community-acquired S. aureus strains, and fibril formation was dependent on expression of the S. aureus δ-toxin gene ( hld ). Mass spectrometry data confirmed that the amyloid fibrils were comprised of δ-toxin. Although S. aureus MVs were produced in vivo in a localized murine infection model, amyloid fibrils were not observed in the in vivo setting. Our findings provide critical insights into staphylococcal factors involved in MV biogenesis and amyloid formation.
Extracellular membrane vesicles (MVs) produced by in planktonic cultures encapsulate a diverse cargo of bacterial proteins, nucleic acids, and glycopolymers that are protected from destruction by external factors. δ-toxin, a member of the phenol soluble modulin family, was shown to be critical for MV biogenesis. Amyloid fibrils co-purified with MVs generated by virulent, community-acquired strains, and fibril formation was dependent on expression of the δ-toxin gene ( ). Mass spectrometry data confirmed that the amyloid fibrils were comprised of δ-toxin. Although MVs were produced in a localized murine infection model, amyloid fibrils were not observed in the setting. Our findings provide critical insights into staphylococcal factors involved in MV biogenesis and amyloid formation.
Author Wang, Xiaogang
Burgin, Dylan J
Otto, Michael
Lee, Jean C
Uppu, Divakara Ssm
Dickey, Seth W
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Cites_doi 10.1128/JB.00642-09
10.1016/j.str.2019.12.006
10.1038/s41596-019-0236-5
10.1371/journal.pone.0040411
10.1038/s41467-017-02448-6
10.1073/pnas.1521230113
10.1038/nm.3047
10.1002/pmic.200900338
10.1002/jev2.12080
10.1016/j.molcel.2008.08.005
10.1038/nrmicro3161
10.1074/jbc.RA118.006472
10.1038/s41586-018-0616-y
10.7554/eLife.59776
10.1021/acsomega.1c02333
10.1128/CMR.00134-14
10.1073/pnas.0900743106
10.1007/978-3-319-72063-0
10.1111/1574-6976.12057
10.1080/21505594.2021.1928395
10.1016/j.micpath.2019.103603
10.1073/pnas.0405620102
10.1038/s41586-020-2066-6
10.1016/j.ijmm.2017.08.010
10.1038/s41467-018-03847-z
10.1074/jbc.M110.167312
10.1128/IAI.00258-15
10.1093/infdis/jit800
10.1016/j.micpath.2016.02.014
10.1002/art.21208
10.1038/s41598-020-64952-y
10.3390/toxins11030178
10.1371/journal.pone.0164523
10.1371/journal.pone.0100499
10.1371/journal.ppat.1002606
10.3389/fmicb.2018.00262
10.1038/nm1656
10.1371/journal.ppat.1002744
10.1128/AAC.01439-18
10.1073/pnas.1115006109
10.1002/mbo3.55
10.1139/o59-099
10.1038/s41467-018-05490-0
10.1016/j.mib.2013.11.004
10.1016/j.bbapap.2010.04.001
10.1371/journal.pone.0027958
10.1128/JB.00300-08
10.1073/pnas.1915829117
10.1128/microbiolspec.VMBF-0012-2015
10.1128/IAI.06014-11
10.3390/microorganisms9010117
10.1128/IAI.00688-09
10.1111/mmi.13219
10.1016/j.jmb.2019.03.030
10.1038/nrmicro3110
10.1590/1414-431X20186773
10.1073/pnas.2121586119
10.1086/657419
10.1128/JB.185.22.6686-6694.2003
10.1038/s41598-020-75108-3
10.3389/fmicb.2016.01404
10.1080/13506129.2021.1960501
10.1111/j.1398-9995.2010.02483.x
10.1128/mBio.01851-18
10.3390/toxins13020075
10.1080/19336896.2019.1704612
10.1128/iai.20.2.388-392.1978
10.3389/fcimb.2018.00277
10.1128/AAC.00522-12
10.1016/j.chom.2010.05.012
10.1038/nrm.2017.125
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Issue 5
Keywords phenol-soluble modulins
delta-toxin
amyloid fibrils
extracellular membrane vesicles
Staphylococcus aureus
Language English
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References 36993475 - bioRxiv. 2023 Mar 23
Tulkens, J, De Wever, O, Hendrix, A (B68) 2020; 15
Pasztor, L, Ziebandt, A-K, Nega, M, Schlag, M, Haase, S, Franz-Wachtel, M, Madlung, J, Nordheim, A, Heinrichs, DE, Götz, F (B42) 2010; 285
Cheung, GYC, Joo, H-S, Chatterjee, SS, Otto, M (B29) 2014; 38
Tong, SYC, Davis, JS, Eichenberger, E, Holland, TL, Fowler, VG (B1) 2015; 28
Sass, V, Schneider, T, Wilmes, M, Körner, C, Tossi, A, Novikova, N, Shamova, O, Sahl, H-G (B25) 2010; 78
Kolar, SL, Ibarra, JA, Rivera, FE, Mootz, JM, Davenport, JE, Stevens, SM, Horswill, AR, Shaw, LN (B7) 2013; 2
Kwon, HI, Jeong, NH, Kim, SY, Kim, MH, Son, JH, Jun, SH, Kim, S, Jeon, H, Kang, SC, Kim, SH, Lee, JC (B21) 2019; 134
Gurung, M, Moon, DC, Choi, CW, Lee, JH, Bae, YC, Kim, J, Lee, YC, Seol, SY, Cho, DT, Kim, SI, Lee, JC (B12) 2011; 6
Shahmirzadi, SV, Nguyen, M-T, Götz, F (B5) 2016; 7
Schwartz, K, Syed, AK, Stephenson, RE, Rickard, AH, Boles, BR, Parsek, MR (B34) 2012; 8
Keller, MD, Ching, KL, Liang, F-X, Dhabaria, A, Tam, K, Ueberheide, BM, Unutmaz, D, Torres, VJ, Cadwell, K (B49) 2020; 579
Green, ER, Mecsas, J (B8) 2016; 4
Dos Santos, DP, Muniz, IPR, Queiroz, AF, Pereira, IS, Souza, MPA, Lima, LJ, Sousa, LRO, Ribeiro, IS, Galantini, MPL, Marques, LM, Figueiredo, TB, da Silva, RAA (B62) 2018; 51
Wilkinson, BJ, Kim, Y, Peterson, PK, Quie, PG, Michael, AF (B70) 1978; 20
Tartaglia, NR, Nicolas, A, Rodovalho, V de R, Luz, B da, Briard-Bion, V, Krupova, Z, Thierry, A, Coste, F, Burel, A, Martin, P, Jardin, J, Azevedo, V, Le Loir, Y, Guédon, E (B17) 2020; 10
Deatherage, BL, Cookson, BT (B18) 2012; 80
Lee, J, Lee, EY, Kim, SH, Kim, DK, Park, KS, Kim, KP, Kim, YK, Roh, TY, Gho, YS (B27) 2013; 57
Siboo, IR, Chaffin, DO, Rubens, CE, Sullam, PM (B9) 2008; 190
Bitto, NJ, Cheng, L, Johnston, EL, Pathirana, R, Phan, TK, Poon, IKH, O’Brien-Simpson, NM, Hill, AF, Stinear, TP, Kaparakis-Liaskos, M (B37) 2021; 10
BLIGH, EG, DYER, WJ (B71) 1959; 37
Kreutzberger, MAB, Wang, S, Beltran, LC, Tuachi, A, Zuo, X, Egelman, EH, Conticello, VP (B32) 2022; 119
Chiappini, N, Seubert, A, Telford, JL, Grandi, G, Serruto, D, Margarit, I, Janulczyk, R (B63) 2012; 7
Piewngam, P, Zheng, Y, Nguyen, TH, Dickey, SW, Joo, H-S, Villaruz, AE, Glose, KA, Fisher, EL, Hunt, RL, Li, B, Chiou, J, Pharkjaksu, S, Khongthong, S, Cheung, GYC, Kiratisin, P, Otto, M (B67) 2018; 562
Salinas, N, Colletier, J-P, Moshe, A, Landau, M (B35) 2018; 9
Schwartz, K, Ganesan, M, Payne, DE, Solomon, MJ, Boles, BR (B45) 2016; 99
Wang, R, Braughton, KR, Kretschmer, D, Bach, T-H, Queck, SY, Li, M, Kennedy, AD, Dorward, DW, Klebanoff, SJ, Peschel, A, DeLeo, FR, Otto, M (B28) 2007; 13
Najarzadeh, Z, Nielsen, J, Farzadfard, A, Sereikaite, V, Strømgaard, K, Meyer, RL, Otzen, DE (B65) 2021; 6
Krakauer, T (B6) 2019; 11
Andreoni, F, Toyofuku, M, Menzi, C, Kalawong, R, Mairpady Shambat, S, François, P, Zinkernagel, AS, Eberl, L (B24) 2019; 63
Wacker, M, Wang, L, Kowarik, M, Dowd, M, Lipowsky, G, Faridmoayer, A, Shields, K, Park, S, Alaimo, C, Kelley, KA, Braun, M, Quebatte, J, Gambillara, V, Carranza, P, Steffen, M, Lee, JC (B69) 2014; 209
Hong, S-W, Kim, M-R, Lee, E-Y, Kim, JH, Kim, Y-S, Jeon, SG, Yang, J-M, Lee, B-J, Pyun, B-Y, Gho, YS, Kim, Y-K (B20) 2011; 66
Tayeb-Fligelman, E, Salinas, N, Tabachnikov, O, Landau, M (B39) 2020; 28
Burts, ML, Williams, WA, DeBord, K, Missiakas, DM (B11) 2005; 102
Wang, X, Koffi, PF, English, OF, Lee, JC (B26) 2021; 13
Zheng, Y, Joo, H-S, Nair, V, Le, KY, Otto, M (B40) 2018; 308
Lee, E-Y, Choi, D-Y, Kim, D-K, Kim, J-W, Park, JO, Kim, S, Kim, S-H, Desiderio, DM, Kim, Y-K, Kim, K-P, Gho, YS (B13) 2009; 9
Tartaglia, NR, Breyne, K, Meyer, E, Cauty, C, Jardin, J, Chrétien, D, Dupont, A, Demeyere, K, Berkova, N, Azevedo, V, Guédon, E, Le Loir, Y (B22) 2018; 8
Wang, X, Eagen, WJ, Lee, JC (B16) 2020; 117
Le, KY, Villaruz, AE, Zheng, Y, He, L, Fisher, EL, Nguyen, TH, Ho, TV, Yeh, AJ, Joo, H-S, Cheung, GYC, Otto, M (B51) 2019; 431
Weidenmaier, C, Lee, JC (B2) 2016; 409
Coelho, C, Brown, L, Maryam, M, Vij, R, Smith, DFQ, Burnet, MC, Kyle, JE, Heyman, HM, Ramirez, J, Prados-Rosales, R, Lauvau, G, Nakayasu, ES, Brady, NR, Hamacher-Brady, A, Coppens, I, Casadevall, A (B47) 2019; 294
Zhou, X, Zheng, Y, Lv, Q, Kong, D, Ji, B, Han, X, Zhou, D, Sun, Z, Zhu, L, Liu, P, Jiang, H, Jiang, Y (B52) 2021; 12
Delano, DL, Montesinos, MC, Desai, A, Wilder, T, Fernandez, P, D’Eustachio, P, Wiltshire, T, Cronstein, BN (B61) 2005; 52
Jeon, H, Oh, MH, Jun, SH, Kim, SI, Choi, CW, Kwon, HI, Na, SH, Kim, YJ, Nicholas, A, Selasi, GN, Lee, JC (B15) 2016; 93
Li, M, Diep, BA, Villaruz, AE, Braughton, KR, Jiang, X, DeLeo, FR, Chambers, HF, Lu, Y, Otto, M (B55) 2009; 106
van Niel, G, D’Angelo, G, Raposo, G (B46) 2018; 19
Askarian, F, Lapek, JD, Dongre, M, Tsai, C-M, Kumaraswamy, M, Kousha, A, Valderrama, JA, Ludviksen, JA, Cavanagh, JP, Uchiyama, S, Mollnes, TE, Gonzalez, DJ, Wai, SN, Nizet, V, Johannessen, M (B23) 2018; 9
Zaman, M, Andreasen, M (B36) 2020; 9
Wang, X, Thompson, CD, Weidenmaier, C, Lee, JC (B14) 2018; 9
Kretschmer, D, Gleske, A-K, Rautenberg, M, Wang, R, Köberle, M, Bohn, E, Schöneberg, T, Rabiet, M-J, Boulay, F, Klebanoff, SJ, van Kessel, KA, van Strijp, JA, Otto, M, Peschel, A (B50) 2010; 7
Surewaard, BGJ, Nijland, R, Spaan, AN, Kruijtzer, JAW, de Haas, CJC, van Strijp, JAG (B66) 2012; 8
Periasamy, S, Joo, H-S, Duong, AC, Bach, T-H, Tan, VY, Chatterjee, SS, Cheung, GYC, Otto, M (B44) 2012; 109
Biancalana, M, Koide, S (B38) 2010; 1804
Hong, S-W, Choi, E-B, Min, T-K, Kim, J-H, Kim, M-H, Jeon, SG, Lee, B-J, Gho, YS, Jee, Y-K, Pyun, B-Y, Kim, Y-K (B19) 2014; 9
Torre, A, Bacconi, M, Sammicheli, C, Galletti, B, Laera, D, Fontana, MR, Grandi, G, De Gregorio, E, Bagnoli, F, Nuti, S, Bertholet, S, Bensi, G (B64) 2015; 83
Blake, KJ, Baral, P, Voisin, T, Lubkin, A, Pinho-Ribeiro, FA, Adams, KL, Roberson, DP, Ma, YC, Otto, M, Woolf, CJ, Torres, VJ, Chiu, IM (B41) 2018; 9
Somerville, GA, Cockayne, A, Dürr, M, Peschel, A, Otto, M, Musser, JM (B53) 2003; 185
Otto, M (B3) 2014; 17
Kowal, J, Arras, G, Colombo, M, Jouve, M, Morath, JP, Primdal-Bengtson, B, Dingli, F, Loew, D, Tkach, M, Théry, C (B48) 2016; 113
Biswas, L, Biswas, R, Nerz, C, Ohlsen, K, Schlag, M, Schäfer, T, Lamkemeyer, T, Ziebandt, A-K, Hantke, K, Rosenstein, R, Götz, F (B10) 2009; 191
Peschel, A, Otto, M (B30) 2013; 11
Chatterjee, SS, Joo, H-S, Duong, AC, Dieringer, TD, Tan, VY, Song, Y, Fischer, ER, Cheung, GYC, Li, M, Otto, M (B54) 2013; 19
Rodriguez, BV, Kuehn, MJ (B57) 2020; 10
Kushnirov, VV, Dergalev, AA, Alexandrov, AI (B58) 2020; 14
Schlatterer, K, Beck, C, Hanzelmann, D, Lebtig, M, Fehrenbacher, B, Schaller, M, Ebner, P, Nega, M, Otto, M, Kretschmer, D, Peschel, A (B31) 2018; 9
Foster, TJ, Geoghegan, JA, Ganesh, VK, Höök, M (B4) 2014; 12
Kizaki, H, Omae, Y, Tabuchi, F, Saito, Y, Sekimizu, K, Kaito, C (B43) 2016; 11
Zaman, M, Andreasen, M (B33) 2021; 9
Schönfelder, J, Pfeiffer, PB, Pradhan, T, Bijzet, J, Hazenberg, BPC, Schönland, SO, Hegenbart, U, Reif, B, Haupt, C, Fändrich, M (B59) 2021; 28
Li, M, Cheung, GYC, Hu, J, Wang, D, Joo, H-S, Deleo, FR, Otto, M (B56) 2010; 202
Queck, SY, Jameson-Lee, M, Villaruz, AE, Bach, T-H, Khan, BA, Sturdevant, DE, Ricklefs, SM, Li, M, Otto, M (B60) 2008; 32
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References_xml – volume: 191
  start-page: 5921
  year: 2009
  end-page: 5929
  ident: B10
  article-title: Role of the twin-arginine translocation pathway in Staphylococcus
  publication-title: J Bacteriol
  doi: 10.1128/JB.00642-09
  contributor:
    fullname: Götz, F
– volume: 28
  start-page: 301
  year: 2020
  end-page: 313
  ident: B39
  article-title: Staphylococcus aureus PSMalpha3 cross-alpha Fibril polymorphism and determinants of cytotoxicity
  publication-title: Structure
  doi: 10.1016/j.str.2019.12.006
  contributor:
    fullname: Landau, M
– volume: 15
  start-page: 40
  year: 2020
  end-page: 67
  ident: B68
  article-title: Analyzing bacterial extracellular vesicles in human body fluids by orthogonal biophysical separation and biochemical characterization
  publication-title: Nat Protoc
  doi: 10.1038/s41596-019-0236-5
  contributor:
    fullname: Hendrix, A
– volume: 7
  year: 2012
  ident: B63
  article-title: Streptococcus pyogenes spycep influences host-pathogen interactions during infection in a murine air pouch model
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0040411
  contributor:
    fullname: Janulczyk, R
– volume: 9
  start-page: 37
  year: 2018
  ident: B41
  article-title: Staphylococcus aureus produces pain through pore-forming toxins and neuronal TRPV1 that is silenced by QX-314
  publication-title: Nat Commun
  doi: 10.1038/s41467-017-02448-6
  contributor:
    fullname: Chiu, IM
– volume: 113
  start-page: E968
  year: 2016
  end-page: 77
  ident: B48
  article-title: Proteomic comparison defines novel markers to characterize heterogeneous populations of extracellular vesicle subtypes
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.1521230113
  contributor:
    fullname: Théry, C
– volume: 19
  start-page: 364
  year: 2013
  end-page: 367
  ident: B54
  article-title: Essential Staphylococcus aureus toxin export system
  publication-title: Nat Med
  doi: 10.1038/nm.3047
  contributor:
    fullname: Otto, M
– volume: 9
  start-page: 5425
  year: 2009
  end-page: 5436
  ident: B13
  article-title: Gram-positive bacteria produce membrane vesicles: proteomics-based characterization of Staphylococcus aureus-derived membrane vesicles
  publication-title: Proteomics
  doi: 10.1002/pmic.200900338
  contributor:
    fullname: Gho, YS
– volume: 10
  year: 2021
  ident: B37
  article-title: Staphylococcus aureus membrane vesicles contain immunostimulatory DNA, RNA and peptidoglycan that activate innate immune receptors and induce autophagy
  publication-title: J Extracell Vesicles
  doi: 10.1002/jev2.12080
  contributor:
    fullname: Kaparakis-Liaskos, M
– volume: 32
  start-page: 150
  year: 2008
  end-page: 158
  ident: B60
  article-title: RNAIII-independent target gene control by the agr quorum-sensing system: insight into the evolution of virulence regulation in Staphylococcus aureus
  publication-title: Mol Cell
  doi: 10.1016/j.molcel.2008.08.005
  contributor:
    fullname: Otto, M
– volume: 12
  start-page: 49
  year: 2014
  end-page: 62
  ident: B4
  article-title: Adhesion, invasion and evasion: the many functions of the surface proteins of Staphylococcus aureus
  publication-title: Nat Rev Microbiol
  doi: 10.1038/nrmicro3161
  contributor:
    fullname: Höök, M
– volume: 294
  start-page: 1202
  year: 2019
  end-page: 1217
  ident: B47
  article-title: Listeria monocytogenes virulence factors, including listeriolysin O, are secreted in biologically active extracellular vesicles
  publication-title: J Biol Chem
  doi: 10.1074/jbc.RA118.006472
  contributor:
    fullname: Casadevall, A
– volume: 562
  start-page: 532
  year: 2018
  end-page: 537
  ident: B67
  article-title: Pathogen elimination by probiotic bacillus via signalling interference
  publication-title: Nature
  doi: 10.1038/s41586-018-0616-y
  contributor:
    fullname: Otto, M
– volume: 9
  year: 2020
  ident: B36
  article-title: Cross-talk between individual phenol-soluble modulins in Staphylococcus aureus biofilm enables rapid and efficient amyloid formation
  publication-title: Elife
  doi: 10.7554/eLife.59776
  contributor:
    fullname: Andreasen, M
– volume: 6
  start-page: 21960
  year: 2021
  end-page: 21970
  ident: B65
  article-title: Human fibrinogen inhibits amyloid assembly of most phenol-soluble modulins from Staphylococcus aureus
  publication-title: ACS Omega
  doi: 10.1021/acsomega.1c02333
  contributor:
    fullname: Otzen, DE
– volume: 28
  start-page: 603
  year: 2015
  end-page: 661
  ident: B1
  article-title: Staphylococcus aureus infections: epidemiology, pathophysiology, clinical manifestations, and management
  publication-title: Clin Microbiol Rev
  doi: 10.1128/CMR.00134-14
  contributor:
    fullname: Fowler, VG
– volume: 106
  start-page: 5883
  year: 2009
  end-page: 5888
  ident: B55
  article-title: Evolution of virulence in epidemic community-associated methicillin-resistant Staphylococcus aureus
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.0900743106
  contributor:
    fullname: Otto, M
– volume: 409
  start-page: 57
  year: 2016
  end-page: 93
  ident: B2
  article-title: Structure and function of surface polysaccharides of Staphylococcus aureus
  publication-title: Curr Top Microbiol Immunol
  doi: 10.1007/978-3-319-72063-0
  contributor:
    fullname: Lee, JC
– volume: 38
  start-page: 698
  year: 2014
  end-page: 719
  ident: B29
  article-title: Phenol-soluble modulins--critical determinants of staphylococcal virulence
  publication-title: FEMS Microbiol Rev
  doi: 10.1111/1574-6976.12057
  contributor:
    fullname: Otto, M
– volume: 12
  start-page: 1418
  year: 2021
  end-page: 1437
  ident: B52
  article-title: Staphylococcus aureus N-terminus formylated δ-toxin tends to form amyloid fibrils, while the deformylated -toxin tends to form functional oligomer complexes
  publication-title: Virulence
  doi: 10.1080/21505594.2021.1928395
  contributor:
    fullname: Jiang, Y
– volume: 134
  start-page: 103603
  year: 2019
  ident: B21
  article-title: Inhibitory effects of thymol on the cytotoxicity and inflammatory responses induced by Staphylococcus aureus extracellular vesicles in cultured keratinocytes
  publication-title: Microb Pathog
  doi: 10.1016/j.micpath.2019.103603
  contributor:
    fullname: Lee, JC
– volume: 102
  start-page: 1169
  year: 2005
  end-page: 1174
  ident: B11
  article-title: Esxa and Esxb are secreted by an ESAT-6-like system that is required for the pathogenesis of Staphylococcus aureus infections
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.0405620102
  contributor:
    fullname: Missiakas, DM
– volume: 579
  start-page: 260
  year: 2020
  end-page: 264
  ident: B49
  article-title: Decoy exosomes provide protection against bacterial toxins
  publication-title: Nature
  doi: 10.1038/s41586-020-2066-6
  contributor:
    fullname: Cadwell, K
– volume: 308
  start-page: 675
  year: 2018
  end-page: 682
  ident: B40
  article-title: Do amyloid structures formed by Staphylococcus aureus phenol-soluble modulins have a biological function?
  publication-title: Int J Med Microbiol
  doi: 10.1016/j.ijmm.2017.08.010
  contributor:
    fullname: Otto, M
– volume: 9
  start-page: 1379
  year: 2018
  ident: B14
  article-title: Release of Staphylococcus aureus extracellular vesicles and their application as a vaccine platform
  publication-title: Nat Commun
  doi: 10.1038/s41467-018-03847-z
  contributor:
    fullname: Lee, JC
– volume: 285
  start-page: 36794
  year: 2010
  end-page: 36803
  ident: B42
  article-title: Staphylococcal major autolysin (atl) is involved in excretion of cytoplasmic proteins
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M110.167312
  contributor:
    fullname: Götz, F
– volume: 83
  start-page: 3157
  year: 2015
  end-page: 3163
  ident: B64
  article-title: Four-component Staphylococcus aureus vaccine 4C-staph enhances Fcgamma receptor expression in neutrophils and monocytes and mitigates S. aureus infection in neutropenic mice
  publication-title: Infect Immun
  doi: 10.1128/IAI.00258-15
  contributor:
    fullname: Bensi, G
– volume: 209
  start-page: 1551
  year: 2014
  end-page: 1561
  ident: B69
  article-title: Prevention of Staphylococcus aureus infections by glycoprotein vaccines synthesized in Escherichia coli
  publication-title: J Infect Dis
  doi: 10.1093/infdis/jit800
  contributor:
    fullname: Lee, JC
– volume: 93
  start-page: 185
  year: 2016
  end-page: 193
  ident: B15
  article-title: Variation among Staphylococcus aureus membrane vesicle proteomes affects cytotoxicity of host cells
  publication-title: Microb Pathog
  doi: 10.1016/j.micpath.2016.02.014
  contributor:
    fullname: Lee, JC
– volume: 52
  start-page: 2567
  year: 2005
  end-page: 2575
  ident: B61
  article-title: Genetically based resistance to the antiinflammatory effects of methotrexate in the air-pouch model of acute inflammation
  publication-title: Arthritis Rheum
  doi: 10.1002/art.21208
  contributor:
    fullname: Cronstein, BN
– volume: 10
  start-page: 8467
  year: 2020
  ident: B17
  article-title: Extracellular vesicles produced by human and animal Staphylococcus aureus strains share a highly conserved core proteome
  publication-title: Sci Rep
  doi: 10.1038/s41598-020-64952-y
  contributor:
    fullname: Guédon, E
– volume: 11
  year: 2019
  ident: B6
  article-title: Staphylococcal superantigens: pyrogenic toxins induce toxic shock
  publication-title: Toxins (Basel)
  doi: 10.3390/toxins11030178
  contributor:
    fullname: Krakauer, T
– volume: 11
  year: 2016
  ident: B43
  article-title: Cell-surface phenol soluble modulins regulate Staphylococcus aureus colony spreading
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0164523
  contributor:
    fullname: Kaito, C
– volume: 9
  year: 2014
  ident: B19
  article-title: An important role of alpha-hemolysin in extracellular vesicles on the development of atopic dermatitis induced by Staphylococcus aureus
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0100499
  contributor:
    fullname: Kim, Y-K
– volume: 8
  year: 2012
  ident: B66
  article-title: Inactivation of staphylococcal phenol soluble modulins by serum lipoprotein particles
  publication-title: PLoS Pathog
  doi: 10.1371/journal.ppat.1002606
  contributor:
    fullname: van Strijp, JAG
– volume: 9
  start-page: 262
  year: 2018
  ident: B23
  article-title: Staphylococcus aureus membrane-derived vesicles promote bacterial virulence and confer protective immunity in murine infection models
  publication-title: Front Microbiol
  doi: 10.3389/fmicb.2018.00262
  contributor:
    fullname: Johannessen, M
– volume: 13
  start-page: 1510
  year: 2007
  end-page: 1514
  ident: B28
  article-title: Identification of novel cytolytic peptides as key virulence determinants for community-associated MRSA
  publication-title: Nat Med
  doi: 10.1038/nm1656
  contributor:
    fullname: Otto, M
– volume: 8
  year: 2012
  ident: B34
  article-title: Functional amyloids composed of phenol soluble modulins stabilize Staphylococcus aureus biofilms
  publication-title: PLoS Pathog
  doi: 10.1371/journal.ppat.1002744
  contributor:
    fullname: Parsek, MR
– volume: 63
  year: 2019
  ident: B24
  article-title: Antibiotics stimulate formation of vesicles in Staphylococcus aureus in both phage-dependent and -independent fashions and via different routes
  publication-title: Antimicrob Agents Chemother
  doi: 10.1128/AAC.01439-18
  contributor:
    fullname: Eberl, L
– volume: 109
  start-page: 1281
  year: 2012
  end-page: 1286
  ident: B44
  article-title: How Staphylococcus aureus biofilms develop their characteristic structure
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.1115006109
  contributor:
    fullname: Otto, M
– volume: 2
  start-page: 18
  year: 2013
  end-page: 34
  ident: B7
  article-title: Extracellular proteases are key mediators of Staphylococcus aureus virulence via the global modulation of virulence-determinant stability
  publication-title: Microbiologyopen
  doi: 10.1002/mbo3.55
  contributor:
    fullname: Shaw, LN
– volume: 37
  start-page: 911
  year: 1959
  end-page: 917
  ident: B71
  article-title: A rapid method of total lipid extraction and purification
  publication-title: Can J Biochem Physiol
  doi: 10.1139/o59-099
  contributor:
    fullname: DYER, WJ
– volume: 9
  start-page: 3512
  year: 2018
  ident: B35
  article-title: Extreme amyloid polymorphism in Staphylococcus aureus virulent PSMalpha peptides
  publication-title: Nat Commun
  doi: 10.1038/s41467-018-05490-0
  contributor:
    fullname: Landau, M
– volume: 17
  start-page: 32
  year: 2014
  end-page: 37
  ident: B3
  article-title: Staphylococcus aureus toxins
  publication-title: Curr Opin Microbiol
  doi: 10.1016/j.mib.2013.11.004
  contributor:
    fullname: Otto, M
– volume: 1804
  start-page: 1405
  year: 2010
  end-page: 1412
  ident: B38
  article-title: Molecular mechanism of thioflavin-T binding to amyloid fibrils
  publication-title: Biochim Biophys Acta
  doi: 10.1016/j.bbapap.2010.04.001
  contributor:
    fullname: Koide, S
– volume: 6
  year: 2011
  ident: B12
  article-title: Staphylococcus aureus produces membrane-derived Vesicles that induce host cell death
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0027958
  contributor:
    fullname: Lee, JC
– volume: 190
  start-page: 6188
  year: 2008
  end-page: 6196
  ident: B9
  article-title: Characterization of the accessory SEC system of Staphylococcus aureus
  publication-title: J Bacteriol
  doi: 10.1128/JB.00300-08
  contributor:
    fullname: Sullam, PM
– volume: 117
  start-page: 3174
  year: 2020
  end-page: 3184
  ident: B16
  article-title: Orchestration of human macrophage Nlrp3 inflammasome activation by Staphylococcus aureus extracellular vesicles
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.1915829117
  contributor:
    fullname: Lee, JC
– volume: 4
  year: 2016
  ident: B8
  article-title: Bacterial secretion systems: an overview
  publication-title: Microbiol Spectr
  doi: 10.1128/microbiolspec.VMBF-0012-2015
  contributor:
    fullname: Mecsas, J
– volume: 80
  start-page: 1948
  year: 2012
  end-page: 1957
  ident: B18
  article-title: Membrane vesicle release in bacteria, eukaryotes, and archaea: a conserved yet underappreciated aspect of microbial life
  publication-title: Infect Immun
  doi: 10.1128/IAI.06014-11
  contributor:
    fullname: Cookson, BT
– volume: 9
  year: 2021
  ident: B33
  article-title: Modulating kinetics of the amyloid-like aggregation of S. aureus phenol-soluble modulins by changes in pH
  publication-title: Microorganisms
  doi: 10.3390/microorganisms9010117
  contributor:
    fullname: Andreasen, M
– volume: 78
  start-page: 2793
  year: 2010
  end-page: 2800
  ident: B25
  article-title: Human beta-defensin 3 inhibits cell wall biosynthesis in Staphylococci
  publication-title: Infect Immun
  doi: 10.1128/IAI.00688-09
  contributor:
    fullname: Sahl, H-G
– volume: 99
  start-page: 123
  year: 2016
  end-page: 134
  ident: B45
  article-title: Extracellular DNA facilitates the formation of functional amyloids in Staphylococcus aureus biofilms
  publication-title: Mol Microbiol
  doi: 10.1111/mmi.13219
  contributor:
    fullname: Boles, BR
– volume: 431
  start-page: 3015
  year: 2019
  end-page: 3027
  ident: B51
  article-title: Role of phenol-soluble modulins in Staphylococcus epidermidis biofilm formation and infection of indwelling medical devices
  publication-title: J Mol Biol
  doi: 10.1016/j.jmb.2019.03.030
  contributor:
    fullname: Otto, M
– volume: 11
  start-page: 667
  year: 2013
  end-page: 673
  ident: B30
  article-title: Phenol-soluble modulins and staphylococcal infection
  publication-title: Nat Rev Microbiol
  doi: 10.1038/nrmicro3110
  contributor:
    fullname: Otto, M
– volume: 51
  year: 2018
  ident: B62
  article-title: Individual variation is the key to the development of a vaccine against Staphylococcus aureus: a comparative study between mice lineages
  publication-title: Braz J Med Biol Res
  doi: 10.1590/1414-431X20186773
  contributor:
    fullname: da Silva, RAA
– volume: 119
  year: 2022
  ident: B32
  article-title: Phenol-soluble modulins PSMalpha3 and PSMbeta2 form nanotubes that are cross-alpha amyloids
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.2121586119
  contributor:
    fullname: Conticello, VP
– volume: 202
  start-page: 1866
  year: 2010
  end-page: 1876
  ident: B56
  article-title: Comparative analysis of virulence and toxin expression of global community-associated methicillin-resistant Staphylococcus aureus strains
  publication-title: J Infect Dis
  doi: 10.1086/657419
  contributor:
    fullname: Otto, M
– volume: 185
  start-page: 6686
  year: 2003
  end-page: 6694
  ident: B53
  article-title: Synthesis and deformylation of Staphylococcus aureus delta-toxin are linked to tricarboxylic acid cycle activity
  publication-title: J Bacteriol
  doi: 10.1128/JB.185.22.6686-6694.2003
  contributor:
    fullname: Musser, JM
– volume: 10
  start-page: 18293
  year: 2020
  ident: B57
  article-title: Staphylococcus aureus secretes immunomodulatory RNA and DNA via membrane vesicles
  publication-title: Sci Rep
  doi: 10.1038/s41598-020-75108-3
  contributor:
    fullname: Kuehn, MJ
– volume: 7
  start-page: 1404
  year: 2016
  ident: B5
  article-title: Evaluation of Staphylococcus aureus lipoproteins: role in nutritional acquisition and pathogenicity
  publication-title: Front Microbiol
  doi: 10.3389/fmicb.2016.01404
  contributor:
    fullname: Götz, F
– volume: 28
  start-page: 243
  year: 2021
  end-page: 251
  ident: B59
  article-title: Protease resistance of ex vivo amyloid fibrils implies the proteolytic selection of disease-associated fibril morphologies
  publication-title: Amyloid
  doi: 10.1080/13506129.2021.1960501
  contributor:
    fullname: Fändrich, M
– volume: 66
  start-page: 351
  year: 2011
  end-page: 359
  ident: B20
  article-title: Extracellular vesicles derived from Staphylococcus aureus induce atopic dermatitis-like skin inflammation
  publication-title: Allergy
  doi: 10.1111/j.1398-9995.2010.02483.x
  contributor:
    fullname: Kim, Y-K
– volume: 9
  year: 2018
  ident: B31
  article-title: The mechanism behind bacterial lipoprotein release: phenol-soluble modulins mediate toll-like receptor 2 activation via extracellular vesicle release from Staphylococcus aureus
  publication-title: mBio
  doi: 10.1128/mBio.01851-18
  contributor:
    fullname: Peschel, A
– volume: 13
  year: 2021
  ident: B26
  article-title: Staphylococcus aureus extracellular vesicles: a story of toxicity and the stress of 2020
  publication-title: Toxins (Basel)
  doi: 10.3390/toxins13020075
  contributor:
    fullname: Lee, JC
– volume: 14
  start-page: 11
  year: 2020
  end-page: 19
  ident: B58
  article-title: Proteinase K resistant cores of prions and amyloids
  publication-title: Prion
  doi: 10.1080/19336896.2019.1704612
  contributor:
    fullname: Alexandrov, AI
– volume: 20
  start-page: 388
  year: 1978
  end-page: 392
  ident: B70
  article-title: Activation of complement by cell surface components of Staphylococcus aureus
  publication-title: Infect Immun
  doi: 10.1128/iai.20.2.388-392.1978
  contributor:
    fullname: Michael, AF
– volume: 8
  start-page: 277
  year: 2018
  ident: B22
  article-title: Staphylococcus aureus extracellular vesicles elicit an Immunostimulatory response in vivo on the murine mammary gland
  publication-title: Front Cell Infect Microbiol
  doi: 10.3389/fcimb.2018.00277
  contributor:
    fullname: Le Loir, Y
– volume: 57
  start-page: 2589
  year: 2013
  end-page: 2595
  ident: B27
  article-title: Staphylococcus aureus extracellular vesicles carry biologically active beta-lactamase
  publication-title: Antimicrob Agents Chemother
  doi: 10.1128/AAC.00522-12
  contributor:
    fullname: Gho, YS
– volume: 7
  start-page: 463
  year: 2010
  end-page: 473
  ident: B50
  article-title: Human formyl peptide receptor 2 senses highly pathogenic Staphylococcus aureus
  publication-title: Cell Host Microbe
  doi: 10.1016/j.chom.2010.05.012
  contributor:
    fullname: Peschel, A
– volume: 19
  start-page: 213
  year: 2018
  end-page: 228
  ident: B46
  article-title: Shedding light on the cell biology of extracellular vesicles
  publication-title: Nat Rev Mol Cell Biol
  doi: 10.1038/nrm.2017.125
  contributor:
    fullname: Raposo, G
– ident: e_1_3_4_50_2
  doi: 10.1038/s41586-020-2066-6
– ident: e_1_3_4_4_2
  doi: 10.1016/j.mib.2013.11.004
– ident: e_1_3_4_53_2
  doi: 10.1080/21505594.2021.1928395
– ident: e_1_3_4_19_2
  doi: 10.1128/IAI.06014-11
– ident: e_1_3_4_37_2
  doi: 10.7554/eLife.59776
– ident: e_1_3_4_12_2
  doi: 10.1073/pnas.0405620102
– ident: e_1_3_4_5_2
  doi: 10.1038/nrmicro3161
– ident: e_1_3_4_36_2
  doi: 10.1038/s41467-018-05490-0
– ident: e_1_3_4_28_2
  doi: 10.1128/AAC.00522-12
– ident: e_1_3_4_29_2
  doi: 10.1038/nm1656
– ident: e_1_3_4_8_2
  doi: 10.1002/mbo3.55
– ident: e_1_3_4_34_2
  doi: 10.3390/microorganisms9010117
– ident: e_1_3_4_61_2
  doi: 10.1016/j.molcel.2008.08.005
– ident: e_1_3_4_45_2
  doi: 10.1073/pnas.1115006109
– ident: e_1_3_4_62_2
  doi: 10.1002/art.21208
– ident: e_1_3_4_7_2
  doi: 10.3390/toxins11030178
– ident: e_1_3_4_41_2
  doi: 10.1016/j.ijmm.2017.08.010
– ident: e_1_3_4_10_2
  doi: 10.1128/JB.00300-08
– ident: e_1_3_4_22_2
  doi: 10.1016/j.micpath.2019.103603
– ident: e_1_3_4_27_2
  doi: 10.3390/toxins13020075
– ident: e_1_3_4_47_2
  doi: 10.1038/nrm.2017.125
– ident: e_1_3_4_48_2
  doi: 10.1074/jbc.RA118.006472
– ident: e_1_3_4_56_2
  doi: 10.1073/pnas.0900743106
– ident: e_1_3_4_69_2
  doi: 10.1038/s41596-019-0236-5
– ident: e_1_3_4_55_2
  doi: 10.1038/nm.3047
– ident: e_1_3_4_6_2
  doi: 10.3389/fmicb.2016.01404
– ident: e_1_3_4_16_2
  doi: 10.1016/j.micpath.2016.02.014
– ident: e_1_3_4_70_2
  doi: 10.1093/infdis/jit800
– ident: e_1_3_4_11_2
  doi: 10.1128/JB.00642-09
– ident: e_1_3_4_18_2
  doi: 10.1038/s41598-020-64952-y
– ident: e_1_3_4_40_2
  doi: 10.1016/j.str.2019.12.006
– ident: e_1_3_4_31_2
  doi: 10.1038/nrmicro3110
– ident: e_1_3_4_54_2
  doi: 10.1128/JB.185.22.6686-6694.2003
– ident: e_1_3_4_25_2
  doi: 10.1128/AAC.01439-18
– ident: e_1_3_4_46_2
  doi: 10.1111/mmi.13219
– ident: e_1_3_4_23_2
  doi: 10.3389/fcimb.2018.00277
– ident: e_1_3_4_68_2
  doi: 10.1038/s41586-018-0616-y
– ident: e_1_3_4_66_2
  doi: 10.1021/acsomega.1c02333
– ident: e_1_3_4_51_2
  doi: 10.1016/j.chom.2010.05.012
– ident: e_1_3_4_21_2
  doi: 10.1111/j.1398-9995.2010.02483.x
– ident: e_1_3_4_60_2
  doi: 10.1080/13506129.2021.1960501
– ident: e_1_3_4_67_2
  doi: 10.1371/journal.ppat.1002606
– ident: e_1_3_4_13_2
  doi: 10.1371/journal.pone.0027958
– ident: e_1_3_4_26_2
  doi: 10.1128/IAI.00688-09
– ident: e_1_3_4_39_2
  doi: 10.1016/j.bbapap.2010.04.001
– ident: e_1_3_4_14_2
  doi: 10.1002/pmic.200900338
– ident: e_1_3_4_35_2
  doi: 10.1371/journal.ppat.1002744
– ident: e_1_3_4_15_2
  doi: 10.1038/s41467-018-03847-z
– ident: e_1_3_4_59_2
  doi: 10.1080/19336896.2019.1704612
– ident: e_1_3_4_71_2
  doi: 10.1128/iai.20.2.388-392.1978
– ident: e_1_3_4_2_2
  doi: 10.1128/CMR.00134-14
– ident: e_1_3_4_20_2
  doi: 10.1371/journal.pone.0100499
– ident: e_1_3_4_30_2
  doi: 10.1111/1574-6976.12057
– ident: e_1_3_4_43_2
  doi: 10.1074/jbc.M110.167312
– ident: e_1_3_4_57_2
  doi: 10.1086/657419
– ident: e_1_3_4_63_2
  doi: 10.1590/1414-431X20186773
– ident: e_1_3_4_38_2
  doi: 10.1002/jev2.12080
– ident: e_1_3_4_49_2
  doi: 10.1073/pnas.1521230113
– ident: e_1_3_4_17_2
  doi: 10.1073/pnas.1915829117
– ident: e_1_3_4_42_2
  doi: 10.1038/s41467-017-02448-6
– ident: e_1_3_4_24_2
  doi: 10.3389/fmicb.2018.00262
– ident: e_1_3_4_3_2
  doi: 10.1007/978-3-319-72063-0
– ident: e_1_3_4_9_2
  doi: 10.1128/microbiolspec.VMBF-0012-2015
– ident: e_1_3_4_58_2
  doi: 10.1038/s41598-020-75108-3
– ident: e_1_3_4_65_2
  doi: 10.1128/IAI.00258-15
– ident: e_1_3_4_72_2
  doi: 10.1139/o59-099
– ident: e_1_3_4_52_2
  doi: 10.1016/j.jmb.2019.03.030
– ident: e_1_3_4_32_2
  doi: 10.1128/mBio.01851-18
– ident: e_1_3_4_33_2
  doi: 10.1073/pnas.2121586119
– ident: e_1_3_4_64_2
  doi: 10.1371/journal.pone.0040411
– ident: e_1_3_4_44_2
  doi: 10.1371/journal.pone.0164523
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Snippet Extracellular membrane vesicles (MVs) produced by in planktonic cultures encapsulate a diverse cargo of bacterial proteins, nucleic acids, and glycopolymers...
Staphylococcus aureus secretes phenol-soluble modulins (PSMs), a family of small, amphipathic, secreted peptides with multiple biologic activities....
ABSTRACT Staphylococcus aureus secretes phenol-soluble modulins (PSMs), a family of small, amphipathic, secreted peptides with multiple biologic activities....
IMPORTANCEExtracellular membrane vesicles (MVs) produced by Staphylococcus aureus in planktonic cultures encapsulate a diverse cargo of bacterial proteins,...
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SubjectTerms Amyloid - metabolism
amyloid fibrils
Animals
Bacterial Proteins - metabolism
Bacteriology
delta-toxin
extracellular membrane vesicles
Mice
phenol-soluble modulins
Research Article
Staphylococcal Infections - microbiology
Staphylococcus aureus
Staphylococcus aureus - metabolism
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Title Staphylococcus aureus delta toxin modulates both extracellular membrane vesicle biogenesis and amyloid formation
URI https://www.ncbi.nlm.nih.gov/pubmed/37795985
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