Disarming Pseudomonas aeruginosa Virulence by the Inhibitory Action of 1,10-Phenanthroline-5,6-Dione-Based Compounds: Elastase B (LasB) as a Chemotherapeutic Target
Elastase B (lasB) is a multifunctional metalloenzyme secreted by the gram-negative pathogen , and this enzyme orchestrates several physiopathological events during bacteria-host interplays. LasB is considered to be a potential target for the development of an innovative chemotherapeutic approach, es...
Saved in:
Published in | Frontiers in microbiology Vol. 10; p. 1701 |
---|---|
Main Authors | , , , , , , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Switzerland
Frontiers Media S.A
02.08.2019
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | Elastase B (lasB) is a multifunctional metalloenzyme secreted by the gram-negative pathogen
, and this enzyme orchestrates several physiopathological events during bacteria-host interplays. LasB is considered to be a potential target for the development of an innovative chemotherapeutic approach, especially against multidrug-resistant strains. Recently, our group showed that 1,10-phenanthroline-5,6-dione (phendione), [Ag(phendione)
]ClO
(Ag-phendione) and [Cu(phendione)
](ClO
)
.4H
O (Cu-phendione) had anti-
action against both planktonic- and biofilm-growing cells. In the present work, we have evaluated the effects of these compounds on the (i) interaction with the lasB active site using
approaches, (ii) lasB proteolytic activity by using a specific fluorogenic peptide substrate, (iii)
gene expression by real time-polymerase chain reaction, (iv) lasB protein secretion by immunoblotting, (v) ability to block the damages induced by lasB on a monolayer of lung epithelial cells, and (vi) survivability of
larvae after being challenged with purified lasB and lasB-rich bacterial secretions. Molecular docking analyses revealed that phendione and its Ag
and Cu
complexes were able to interact with the amino acids forming the active site of lasB, particularly Cu-phendione which exhibited the most favorable interaction energy parameters. Additionally, the test compounds were effective inhibitors of lasB activity, blocking the
cleavage of the peptide substrate, aminobenzyl-Ala-Gly-Leu-Ala-
-nitrobenzylamide, with Cu-phendione having the best inhibitory action (K
= 90 nM). Treating living bacteria with a sub-inhibitory concentration (½ × MIC value) of the test compounds caused a significant reduction in the expression of the
gene as well as its mature protein production/secretion. Further, Ag-phendione and Cu-phendione offered protective action for lung epithelial cells, reducing the A549 monolayer damage by approximately 32 and 42%, respectively. Interestingly, Cu-phendione mitigated the toxic effect of both purified lasB molecules and lasB-containing bacterial secretions in the
model, increasing the survival time of
larvae. Collectively, these data reinforce the concept of lasB being a veritable therapeutic target and phendione-based compounds (mainly Cu-phendione) being prospective anti-virulence drugs against
. |
---|---|
AbstractList | Elastase B (lasB) is a multifunctional metalloenzyme secreted by the gram-negative pathogen Pseudomonas aeruginosa, and this enzyme orchestrates several physiopathological events during bacteria-host interplays. LasB is considered to be a potential target for the development of an innovative chemotherapeutic approach, especially against multidrug-resistant strains. Recently, our group showed that 1,10-phenanthroline-5,6-dione (phendione), [Ag(phendione)2]ClO4 (Ag-phendione) and [Cu(phendione)3](ClO4)2.4H2O (Cu-phendione) had anti-P. aeruginosa action against both planktonic- and biofilm-growing cells. In the present work, we have evaluated the effects of these compounds on the (i) interaction with the lasB active site using in silico approaches, (ii) lasB proteolytic activity by using a specific fluorogenic peptide substrate, (iii) lasB gene expression by real time-polymerase chain reaction, (iv) lasB protein secretion by immunoblotting, (v) ability to block the damages induced by lasB on a monolayer of lung epithelial cells, and (vi) survivability of Galleria mellonella larvae after being challenged with purified lasB and lasB-rich bacterial secretions. Molecular docking analyses revealed that phendione and its Ag+ and Cu2+ complexes were able to interact with the amino acids forming the active site of lasB, particularly Cu-phendione which exhibited the most favorable interaction energy parameters. Additionally, the test compounds were effective inhibitors of lasB activity, blocking the in vitro cleavage of the peptide substrate, aminobenzyl-Ala-Gly-Leu-Ala-p-nitrobenzylamide, with Cu-phendione having the best inhibitory action (Ki = 90 nM). Treating living bacteria with a sub-inhibitory concentration (½ × MIC value) of the test compounds caused a significant reduction in the expression of the lasB gene as well as its mature protein production/secretion. Further, Ag-phendione and Cu-phendione offered protective action for lung epithelial cells, reducing the A549 monolayer damage by approximately 32 and 42%, respectively. Interestingly, Cu-phendione mitigated the toxic effect of both purified lasB molecules and lasB-containing bacterial secretions in the in vivo model, increasing the survival time of G. mellonella larvae. Collectively, these data reinforce the concept of lasB being a veritable therapeutic target and phendione-based compounds (mainly Cu-phendione) being prospective anti-virulence drugs against P. aeruginosa. Elastase B (lasB) is a multifunctional metalloenzyme secreted by the gram-negative pathogen , and this enzyme orchestrates several physiopathological events during bacteria-host interplays. LasB is considered to be a potential target for the development of an innovative chemotherapeutic approach, especially against multidrug-resistant strains. Recently, our group showed that 1,10-phenanthroline-5,6-dione (phendione), [Ag(phendione) ]ClO (Ag-phendione) and [Cu(phendione) ](ClO ) .4H O (Cu-phendione) had anti- action against both planktonic- and biofilm-growing cells. In the present work, we have evaluated the effects of these compounds on the (i) interaction with the lasB active site using approaches, (ii) lasB proteolytic activity by using a specific fluorogenic peptide substrate, (iii) gene expression by real time-polymerase chain reaction, (iv) lasB protein secretion by immunoblotting, (v) ability to block the damages induced by lasB on a monolayer of lung epithelial cells, and (vi) survivability of larvae after being challenged with purified lasB and lasB-rich bacterial secretions. Molecular docking analyses revealed that phendione and its Ag and Cu complexes were able to interact with the amino acids forming the active site of lasB, particularly Cu-phendione which exhibited the most favorable interaction energy parameters. Additionally, the test compounds were effective inhibitors of lasB activity, blocking the cleavage of the peptide substrate, aminobenzyl-Ala-Gly-Leu-Ala- -nitrobenzylamide, with Cu-phendione having the best inhibitory action (K = 90 nM). Treating living bacteria with a sub-inhibitory concentration (½ × MIC value) of the test compounds caused a significant reduction in the expression of the gene as well as its mature protein production/secretion. Further, Ag-phendione and Cu-phendione offered protective action for lung epithelial cells, reducing the A549 monolayer damage by approximately 32 and 42%, respectively. Interestingly, Cu-phendione mitigated the toxic effect of both purified lasB molecules and lasB-containing bacterial secretions in the model, increasing the survival time of larvae. Collectively, these data reinforce the concept of lasB being a veritable therapeutic target and phendione-based compounds (mainly Cu-phendione) being prospective anti-virulence drugs against . Elastase B (lasB) is a multifunctional metalloenzyme secreted by the gram-negative pathogen Pseudomonas aeruginosa , and this enzyme orchestrates several physiopathological events during bacteria-host interplays. LasB is considered to be a potential target for the development of an innovative chemotherapeutic approach, especially against multidrug-resistant strains. Recently, our group showed that 1,10-phenanthroline-5,6-dione (phendione), [Ag(phendione) 2 ]ClO 4 (Ag-phendione) and [Cu(phendione) 3 ](ClO 4 ) 2 .4H 2 O (Cu-phendione) had anti- P. aeruginosa action against both planktonic- and biofilm-growing cells. In the present work, we have evaluated the effects of these compounds on the (i) interaction with the lasB active site using in silico approaches, (ii) lasB proteolytic activity by using a specific fluorogenic peptide substrate, (iii) lasB gene expression by real time-polymerase chain reaction, (iv) lasB protein secretion by immunoblotting, (v) ability to block the damages induced by lasB on a monolayer of lung epithelial cells, and (vi) survivability of Galleria mellonella larvae after being challenged with purified lasB and lasB-rich bacterial secretions. Molecular docking analyses revealed that phendione and its Ag + and Cu 2+ complexes were able to interact with the amino acids forming the active site of lasB, particularly Cu-phendione which exhibited the most favorable interaction energy parameters. Additionally, the test compounds were effective inhibitors of lasB activity, blocking the in vitro cleavage of the peptide substrate, aminobenzyl-Ala-Gly-Leu-Ala- p -nitrobenzylamide, with Cu-phendione having the best inhibitory action (K i = 90 nM). Treating living bacteria with a sub-inhibitory concentration (½ × MIC value) of the test compounds caused a significant reduction in the expression of the lasB gene as well as its mature protein production/secretion. Further, Ag-phendione and Cu-phendione offered protective action for lung epithelial cells, reducing the A549 monolayer damage by approximately 32 and 42%, respectively. Interestingly, Cu-phendione mitigated the toxic effect of both purified lasB molecules and lasB-containing bacterial secretions in the in vivo model, increasing the survival time of G. mellonella larvae. Collectively, these data reinforce the concept of lasB being a veritable therapeutic target and phendione-based compounds (mainly Cu-phendione) being prospective anti-virulence drugs against P. aeruginosa . |
Author | Ramalho, Teodorico C O'Shaughnessy, Megan Mello, Thaís P Devereux, Michael de Castro, Alexandre A Galdino, Anna Clara M Howe, Orla Mattos, Larissa M Santos, André L S Hunt, Mary C McCann, Malachy Pereira, Marcos D Viganor, Lívia da Cunha, Elaine F F Branquinha, Marta H |
AuthorAffiliation | 5 Department of Chemistry, Maynooth University , Maynooth , Ireland 1 Department of General Microbiology, Institute of Microbiology Paulo de Góes, Federal University of Rio de Janeiro , Rio de Janeiro , Brazil 3 The Centre for Biomimetic and Therapeutic Research, Focas Research Institute, Technological University Dublin , Dublin , Ireland 2 Postgraduate Program in Biochemistry, Institute of Chemistry, Federal University of Rio de Janeiro , Rio de Janeiro , Brazil 4 Department of Chemistry, Federal University of Lavras , Lavras , Brazil |
AuthorAffiliation_xml | – name: 4 Department of Chemistry, Federal University of Lavras , Lavras , Brazil – name: 5 Department of Chemistry, Maynooth University , Maynooth , Ireland – name: 1 Department of General Microbiology, Institute of Microbiology Paulo de Góes, Federal University of Rio de Janeiro , Rio de Janeiro , Brazil – name: 3 The Centre for Biomimetic and Therapeutic Research, Focas Research Institute, Technological University Dublin , Dublin , Ireland – name: 2 Postgraduate Program in Biochemistry, Institute of Chemistry, Federal University of Rio de Janeiro , Rio de Janeiro , Brazil |
Author_xml | – sequence: 1 givenname: Anna Clara M surname: Galdino fullname: Galdino, Anna Clara M organization: Postgraduate Program in Biochemistry, Institute of Chemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil – sequence: 2 givenname: Lívia surname: Viganor fullname: Viganor, Lívia organization: The Centre for Biomimetic and Therapeutic Research, Focas Research Institute, Technological University Dublin, Dublin, Ireland – sequence: 3 givenname: Alexandre A surname: de Castro fullname: de Castro, Alexandre A organization: Department of Chemistry, Federal University of Lavras, Lavras, Brazil – sequence: 4 givenname: Elaine F F surname: da Cunha fullname: da Cunha, Elaine F F organization: Department of Chemistry, Federal University of Lavras, Lavras, Brazil – sequence: 5 givenname: Thaís P surname: Mello fullname: Mello, Thaís P organization: Department of General Microbiology, Institute of Microbiology Paulo de Góes, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil – sequence: 6 givenname: Larissa M surname: Mattos fullname: Mattos, Larissa M organization: Postgraduate Program in Biochemistry, Institute of Chemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil – sequence: 7 givenname: Marcos D surname: Pereira fullname: Pereira, Marcos D organization: Postgraduate Program in Biochemistry, Institute of Chemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil – sequence: 8 givenname: Mary C surname: Hunt fullname: Hunt, Mary C organization: The Centre for Biomimetic and Therapeutic Research, Focas Research Institute, Technological University Dublin, Dublin, Ireland – sequence: 9 givenname: Megan surname: O'Shaughnessy fullname: O'Shaughnessy, Megan organization: The Centre for Biomimetic and Therapeutic Research, Focas Research Institute, Technological University Dublin, Dublin, Ireland – sequence: 10 givenname: Orla surname: Howe fullname: Howe, Orla organization: The Centre for Biomimetic and Therapeutic Research, Focas Research Institute, Technological University Dublin, Dublin, Ireland – sequence: 11 givenname: Michael surname: Devereux fullname: Devereux, Michael organization: The Centre for Biomimetic and Therapeutic Research, Focas Research Institute, Technological University Dublin, Dublin, Ireland – sequence: 12 givenname: Malachy surname: McCann fullname: McCann, Malachy organization: Department of Chemistry, Maynooth University, Maynooth, Ireland – sequence: 13 givenname: Teodorico C surname: Ramalho fullname: Ramalho, Teodorico C organization: Department of Chemistry, Federal University of Lavras, Lavras, Brazil – sequence: 14 givenname: Marta H surname: Branquinha fullname: Branquinha, Marta H organization: Department of General Microbiology, Institute of Microbiology Paulo de Góes, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil – sequence: 15 givenname: André L S surname: Santos fullname: Santos, André L S organization: Postgraduate Program in Biochemistry, Institute of Chemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/31428062$$D View this record in MEDLINE/PubMed |
BookMark | eNpVkk1P3DAQhqOKqlDKvafKRyqRre0kjtNDJXah7UorlQOterMm9mRjlNiLnVTa_8MPJbtLEfjgGc3H887hfZ8cOe8wST4yOssyWX1peqvrGaesmlFWUvYmOWFC5GlG-d-jF_lxchbjHZ1eTvn0v0uOM5ZzSQU_SR6ubITQW7cmNxFH43vvIBLAMK6t8xHIHxvGDp1GUm_J0CJZutbWdvBhSy71YL0jviHsgtH0pkUHbmiD76zDtLgQ6dXUx3QOEQ1Z-H7jR2fiV3LdQRymIpmT8xXE-WeyEyWLFns_aQTY4DhYTW4hrHH4kLxtoIt49hRPk9_fr28XP9PVrx_LxeUq1bngQ1pBAVwWWZ4X3BSosZSFrGqWS-RCAzeQ180Uq1o2ktW8kbKigCB5iXWuITtNlgeu8XCnNsH2ELbKg1X7gg9rBWE6q0NlitpUtNSiNiw3BZNZY2jDyrw0RuqCT6xvB9ZmrHs0Gt0QoHsFfd1xtlVr_08JISXjYgKcPwGCvx8xDqq3UWPXgUM_RsWzTFQyY7yaRulhVAcfY8DmWYZRtfOK2ntF7byi9l6ZVj69PO954b8zskdeh79R |
CitedBy_id | crossref_primary_10_1007_s00436_021_07265_x crossref_primary_10_1021_acscentsci_3c01102 crossref_primary_10_1007_s00775_022_01979_8 crossref_primary_10_1002_asia_202200866 crossref_primary_10_1016_j_ejmech_2021_113172 crossref_primary_10_52547_JoMMID_9_3_142 crossref_primary_10_1002_adfm_202214852 crossref_primary_10_1111_lam_13485 crossref_primary_10_3390_pathogens9080639 crossref_primary_10_1007_s00253_023_12890_w crossref_primary_10_1038_s41392_022_01056_1 crossref_primary_10_3390_nano10081527 crossref_primary_10_3390_tropicalmed8070348 crossref_primary_10_1016_j_lfs_2020_118878 crossref_primary_10_3390_microorganisms11051345 crossref_primary_10_1371_journal_pone_0258950 crossref_primary_10_3389_fmicb_2020_620819 crossref_primary_10_1016_j_drudis_2021_02_026 crossref_primary_10_2174_1381612829666230413085029 crossref_primary_10_3390_antibiotics12060998 crossref_primary_10_1007_s00203_023_03713_7 crossref_primary_10_3389_fcimb_2022_926758 crossref_primary_10_2147_IDR_S403441 crossref_primary_10_3390_antibiotics12030499 crossref_primary_10_3390_pathogens12010070 crossref_primary_10_1007_s00284_023_03500_z crossref_primary_10_1021_acsmedchemlett_0c00554 crossref_primary_10_1007_s42770_024_01426_7 crossref_primary_10_1016_j_ejmcr_2022_100093 crossref_primary_10_3390_pathogens10060765 crossref_primary_10_3390_ijms222312892 crossref_primary_10_1002_aoc_6695 crossref_primary_10_15252_embr_202256033 crossref_primary_10_3390_pathogens12040609 crossref_primary_10_1093_femspd_ftaa059 crossref_primary_10_3390_antibiotics9100674 crossref_primary_10_3390_ijms241512296 crossref_primary_10_2217_fmb_2022_0202 crossref_primary_10_3390_antibiotics11081060 crossref_primary_10_1007_s00253_021_11637_9 crossref_primary_10_3390_pathogens12050745 |
Cites_doi | 10.1093/jac/dkv292 10.1093/infdis/124.Supplement_1.S59 10.1016/s1286-4579(00)00280-x 10.1099/jmm.0.05132-0 10.1007/s13238-014-0100-x 10.1016/j.bbrc.2012.04.157 10.1155/2016/1321487 10.1371/journal.pone.0075708 10.1016/0003-2697(80)90338-3 10.1038/nprot.2008.73 10.1128/AAC.03063-14 10.2174/092986712800609733 10.2174/1568026616666161003143333 10.1038/nrd.2017.23 10.1167/iovs.04-1483 10.1007/978-981-10-6141-7_16 10.2174/2210303106666160506120057 10.3389/fcimb.2017.00093 10.1016/j.chembiol.2015.03.012 10.1007/bf02789146 10.1038/srep13719 10.1007/s10930-007-9113-0 10.1111/1462-2920.13262 10.1016/j.ijmm.2014.07.001 10.1128/IAI.64.1.37-43.1996 10.2108/zsj.30.345 10.1016/j.drudis.2018.07.003 10.1111/j.1462-5822.2008.01142.x 10.1021/cen-v077n017.p002 10.1016/j.ajic.2016.08.007 10.1164/ajrccm/148.4_pt_1.1061 10.1371/journal.pone.0098162 10.1016/j.enzmictec.2013.09.014 10.1099/jmm.0.009142-0 10.1038/nature17042 10.1007/s10534-004-1229-5 10.1128/mBio.01603-15 10.4155/fsoa-2017-0109 10.1038/nrmicro3232 10.1099/mic.0.26280-0 10.1007/s11274-013-1252-1 10.1016/S1473-3099(17)30753-3 10.1016/S0021-9258(19)52451-6 10.3390/ijms19041257 10.1038/nrmicro3028 10.1016/j.jip.2013.10.006 10.3402/jev.v2i0.20384 10.3389/fmicb.2017.00076 10.1007/s00044-015-1436-3 10.1021/ml300128f 10.3389/fmicb.2017.01257 10.1016/j.funbio.2017.04.002 10.1093/jac/dkq036 10.3390/jof4030113 10.1128/AAC.00776-10 10.1038/35023079 10.1017/S003118201800152X 10.2147/IJN.S141201 10.1093/nar/gks1039 10.21769/BioProtoc.2329 10.1038/s41598-018-37422-9 10.1073/pnas.96.5.2408 10.1016/j.rmed.2017.05.001 10.1186/1465-9921-15-21 10.3390/jof4040128 10.1016/S0021-9258(18)49927-9 10.1128/AAC.00511-10 10.1371/journal.pone.0027091 10.1038/srep09936 10.1021/jm051197e 10.1080/07391102.2013.765361 10.1186/1477-5956-11-44 10.1039/c2tx00010e |
ContentType | Journal Article |
Copyright | Copyright © 2019 Galdino, Viganor, de Castro, da Cunha, Mello, Mattos, Pereira, Hunt, O’Shaughnessy, Howe, Devereux, McCann, Ramalho, Branquinha and Santos. 2019 Galdino, Viganor, de Castro, da Cunha, Mello, Mattos, Pereira, Hunt, O’Shaughnessy, Howe, Devereux, McCann, Ramalho, Branquinha and Santos |
Copyright_xml | – notice: Copyright © 2019 Galdino, Viganor, de Castro, da Cunha, Mello, Mattos, Pereira, Hunt, O’Shaughnessy, Howe, Devereux, McCann, Ramalho, Branquinha and Santos. 2019 Galdino, Viganor, de Castro, da Cunha, Mello, Mattos, Pereira, Hunt, O’Shaughnessy, Howe, Devereux, McCann, Ramalho, Branquinha and Santos |
DBID | NPM AAYXX CITATION 7X8 5PM DOA |
DOI | 10.3389/fmicb.2019.01701 |
DatabaseName | PubMed CrossRef MEDLINE - Academic PubMed Central (Full Participant titles) Directory of Open Access Journals |
DatabaseTitle | PubMed CrossRef MEDLINE - Academic |
DatabaseTitleList | PubMed |
Database_xml | – sequence: 1 dbid: DOA name: Directory of Open Access Journals url: https://www.doaj.org/ sourceTypes: Open Website – sequence: 2 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Biology |
EISSN | 1664-302X |
EndPage | 1701 |
ExternalDocumentID | oai_doaj_org_article_d5bd907c6bd14d5183fd0f1747dd8c52 10_3389_fmicb_2019_01701 31428062 |
Genre | Journal Article |
GrantInformation_xml | – fundername: Conselho Nacional de Desenvolvimento Científico e Tecnológico – fundername: Coordenação de Aperfeiçoamento de Pessoal de Nível Superior – fundername: Fundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de Janeiro |
GroupedDBID | 53G 5VS 9T4 AAFWJ AAKDD ACGFO ACGFS ACXDI ADBBV ADRAZ AENEX ALMA_UNASSIGNED_HOLDINGS AOIJS BAWUL BCNDV DIK ECGQY GROUPED_DOAJ GX1 HYE IAO IEA IHR IPNFZ KQ8 M48 M~E NPM O5R O5S OK1 PGMZT RIG RNS RPM AAYXX CITATION 7X8 5PM AFPKN |
ID | FETCH-LOGICAL-c462t-9a5a28534452d5ece78589b148e26ca2da4bfca29b8f81b2f8890aea827eb4ca3 |
IEDL.DBID | RPM |
ISSN | 1664-302X |
IngestDate | Tue Oct 22 15:14:47 EDT 2024 Tue Sep 17 21:26:50 EDT 2024 Fri Oct 25 01:26:37 EDT 2024 Thu Nov 21 21:28:13 EST 2024 Wed Oct 16 00:48:08 EDT 2024 |
IsDoiOpenAccess | true |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Keywords | Pseudomonas aeruginosa theoretical calculations 1,10-phenanthroline-5,6-dione metal-based compounds anti-virulence therapy elastase B |
Language | English |
License | This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c462t-9a5a28534452d5ece78589b148e26ca2da4bfca29b8f81b2f8890aea827eb4ca3 |
Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Reviewed by: Naoki Hayashi, Kyoto Pharmaceutical University, Japan; César de la Fuente, Massachusetts Institute of Technology, United States Edited by: Zhiyong Zong, West China Hospital, China This article was submitted to Antimicrobials, Resistance and Chemotherapy, a section of the journal Frontiers in Microbiology |
OpenAccessLink | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6688126/ |
PMID | 31428062 |
PQID | 2336983129 |
PQPubID | 23479 |
PageCount | 1 |
ParticipantIDs | doaj_primary_oai_doaj_org_article_d5bd907c6bd14d5183fd0f1747dd8c52 pubmedcentral_primary_oai_pubmedcentral_nih_gov_6688126 proquest_miscellaneous_2336983129 crossref_primary_10_3389_fmicb_2019_01701 pubmed_primary_31428062 |
PublicationCentury | 2000 |
PublicationDate | 2019-08-02 |
PublicationDateYYYYMMDD | 2019-08-02 |
PublicationDate_xml | – month: 08 year: 2019 text: 2019-08-02 day: 02 |
PublicationDecade | 2010 |
PublicationPlace | Switzerland |
PublicationPlace_xml | – name: Switzerland |
PublicationTitle | Frontiers in microbiology |
PublicationTitleAlternate | Front Microbiol |
PublicationYear | 2019 |
Publisher | Frontiers Media S.A |
Publisher_xml | – name: Frontiers Media S.A |
References | McMillan (B42) 2014; 9 Strateva (B63) 2009; 58 Zhu (B76) 2015; 22 Lowry (B36) 1951; 193 Balasubramanian (B9) 2013; 41 Sakata (B54) 1993; 148 Allen (B4) 2014; 12 Andrejko (B6) 2014; 115 Heussen (B25) 1980; 102 Miyoshi (B44) 2000; 2 Medeiros (B43) 1971; 124 Rizzo (B52) 2017; 121 Thomsen (B69) 2006; 49 McCann (B39) 2004; 17 Suarez-Cuartin (B64) 2017; 128 Andrejko (B5) 2013; 30 Carson (B12) 2012; 422 Hwang (B27) 2019; 9 Lutfullah (B37) 2008; 27 Murray (B46) 2015; 6 Yang (B75) 2015; 5 Gandra (B18) 2017; 8 Rosenthal (B53) 2016; 44 Cowell (B14) 2003; 149 McCann (B40); 19 Alipour (B3) 2010; 65 Kawaharajo (B29) 1982; 52 Vanden Bergh (B71) 2013; 11 Rigo (B51) 2018; 12 Fernandes (B16) 2017; 7 Gi (B20) 2014; 58 Granato (B22) 2017; 8 Lemire (B35) 2013; 11 Ventola (B72) 2015; 40 Pereira (B48) 2018; 4 Schmittgen (B56) 2008; 3 Sonmezer (B61) 2016; 2016 Hehre (B24) 1999; 77 Totsika (B70) 2016; 6 Viganor (B73) 2016; 71 McCann (B41); 1 Tang (B67) 1996; 64 Cathcart (B13) 2011; 55 Galdino (B17) 2017 Husain (B26) 2013; 29 Garner (B19) 2012; 3 Tacconelli (B65) 2018; 18 Beaufort (B10) 2013; 8 Morgon (B45) 2007 Aoki (B7) 2010; 54 Ali (B2) 2017; 12 Stover (B62) 2000; 406 Dickey (B15) 2017; 16 Silva (B58) 2015; 24 Lee (B34) 2015; 6 Kavanagh (B28) 2018; 4 Savli (B55) 2003; 52 Kim (B31) 2013; 2 Prateeksha, Singh (B49) 2017; 7 Viganor (B74) 2017; 17 Kuang (B33) 2011; 6 Marquart (B38) 2005; 46 Silva (B57) 2014; 304 Thayer (B68) 1991; 266 Kida (B30) 2008; 10 Nomura (B47) 2014; 15 Singh (B59) 2015; 5 Kocabiyik (B32) 1995; 50 Reboud (B50) 2016; 18 Goncalves (B21) 2014; 32 Soares (B60) 2018; 19 Tan (B66) 1999; 96 Brown (B11) 2016; 529 Azam (B8) 2018; 24 Han (B23) 2014; 54 Ali (B1) 2018; 4 |
References_xml | – volume: 71 start-page: 128 year: 2016 ident: B73 article-title: Anti-Pseudomonas aeruginosa activity of 1,10-phenanthroline-based drugs against both planktonic- and biofilm-growing cells. publication-title: J. Antimicrob. Chemother. doi: 10.1093/jac/dkv292 contributor: fullname: Viganor – volume: 124 start-page: 59 year: 1971 ident: B43 article-title: Effect of salt concentration on the apparent in-vitro susceptibility of Pseudomonas and other gram-negative bacilli to gentamicin. publication-title: J. Infect. Dis. doi: 10.1093/infdis/124.Supplement_1.S59 contributor: fullname: Medeiros – volume: 2 start-page: 91 year: 2000 ident: B44 article-title: Microbial metalloproteases and pathogenesis. publication-title: Microbes Infect. doi: 10.1016/s1286-4579(00)00280-x contributor: fullname: Miyoshi – volume: 52 start-page: 403 year: 2003 ident: B55 article-title: Expression stability of six housekeeping genes: a proposal for resistance gene quantification studies of Pseudomonas aeruginosa by real-time quantitative RT-PCR. publication-title: J. Med. Microbiol. doi: 10.1099/jmm.0.05132-0 contributor: fullname: Savli – volume: 6 start-page: 26 year: 2015 ident: B34 article-title: The hierarchy quorum sensing network in Pseudomonas aeruginosa. publication-title: Protein Cell. doi: 10.1007/s13238-014-0100-x contributor: fullname: Lee – volume: 422 start-page: 316 year: 2012 ident: B12 article-title: Comparison of the binding specificity of two bacterial metalloproteases, LasB of Pseudomonas aeruginosa and ZapA of Proteus mirabilis, using N-alpha mercaptoamide template-based inhibitor analogues. publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2012.04.157 contributor: fullname: Carson – volume: 2016 year: 2016 ident: B61 article-title: Evaluation of risk factors for antibiotic resistance in patients with nosocomial infections caused by Pseudomonas aeruginosa. publication-title: Can. J. Infect. Dis. Med. Microbiol. doi: 10.1155/2016/1321487 contributor: fullname: Sonmezer – volume: 8 year: 2013 ident: B10 article-title: Disruption of the endothelial barrier by proteases from the bacterial pathogen Pseudomonas aeruginosa: implication of matrilysis and receptor cleavage. publication-title: PLoS One doi: 10.1371/journal.pone.0075708 contributor: fullname: Beaufort – volume: 102 start-page: 196 year: 1980 ident: B25 article-title: Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates. publication-title: Anal Biochem. doi: 10.1016/0003-2697(80)90338-3 contributor: fullname: Heussen – volume: 3 start-page: 1101 year: 2008 ident: B56 article-title: Analyzing real-time PCR data by the comparative C(T) method. publication-title: Nat. Protoc. doi: 10.1038/nprot.2008.73 contributor: fullname: Schmittgen – volume: 58 start-page: 7205 year: 2014 ident: B20 article-title: A drug-repositioning screening identifies pentetic acid as a potential therapeutic agent for suppressing the elastase-mediated virulence of Pseudomonas aeruginosa. publication-title: Antimicrob. Agents Chemother. doi: 10.1128/AAC.03063-14 contributor: fullname: Gi – volume: 19 start-page: 2703 ident: B40 article-title: Deciphering the antimicrobial activity of phenanthroline chelators. publication-title: Curr. Med. Chem. doi: 10.2174/092986712800609733 contributor: fullname: McCann – volume: 17 start-page: 1280 year: 2017 ident: B74 article-title: The antibacterial activity of metal complexes containing 1,10-phenantroline: potential as alternative therapeutics in the era of antibiotic resistance. publication-title: Curr. Top. Med. Chem. doi: 10.2174/1568026616666161003143333 contributor: fullname: Viganor – volume: 16 start-page: 457 year: 2017 ident: B15 article-title: Different drugs for bad bugs: antivirulence strategies in the age of antibiotic resistance. publication-title: Nat. Rev. Drug Discov. doi: 10.1038/nrd.2017.23 contributor: fullname: Dickey – volume: 52 start-page: 271 year: 1982 ident: B29 article-title: Effect of phosphoramidon on protection against corneal ulcer caused by elastase and protease from Pseudomonas aeruginosa. publication-title: Jpn. J. Exp. Med. contributor: fullname: Kawaharajo – volume: 46 start-page: 3761 year: 2005 ident: B38 article-title: Identification of a novel secreted protease from Pseudomonas aeruginosa that causes corneal erosions. publication-title: Invest. Ophthalmol. Vis. Sci. doi: 10.1167/iovs.04-1483 contributor: fullname: Marquart – year: 2007 ident: B45 publication-title: Métodos de Química Teórica e Modelagem Molecular. contributor: fullname: Morgon – start-page: 381 year: 2017 ident: B17 article-title: Pseudomonas aeruginosa and its arsenal of proteases: weapons to battle the host publication-title: Pathophysiological Aspects of proteases doi: 10.1007/978-981-10-6141-7_16 contributor: fullname: Galdino – volume: 6 start-page: 30 year: 2016 ident: B70 article-title: Benefits and challenges of antivirulence antimicrobials at the dawn of the post-antibiotic era. publication-title: Curr. Med. Chem. doi: 10.2174/2210303106666160506120057 contributor: fullname: Totsika – volume: 7 year: 2017 ident: B49 article-title: Scaffold of selenium nanovectors and honey phytochemicals for inhibition of Pseudomonas aeruginosa quorum sensing and biofilm formation. publication-title: Front. Cell Infect. Microbiol doi: 10.3389/fcimb.2017.00093 contributor: fullname: Prateeksha, Singh – volume: 22 start-page: 483 year: 2015 ident: B76 article-title: Disarming Pseudomonas aeruginosa virulence factor LasB by leveraging a Caenorhabditis elegans infection model. publication-title: Chem. Biol. doi: 10.1016/j.chembiol.2015.03.012 contributor: fullname: Zhu – volume: 50 start-page: 25 year: 1995 ident: B32 article-title: Effects of metals on elastase from Pseudomonas aeruginosa SES-938-1. publication-title: Biol. Trace. Elem. Res. doi: 10.1007/bf02789146 contributor: fullname: Kocabiyik – volume: 5 year: 2015 ident: B59 article-title: Mycofabricated biosilver nanoparticles interrupt Pseudomonas aeruginosa quorum sensing systems. publication-title: Sci. Rep. doi: 10.1038/srep13719 contributor: fullname: Singh – volume: 27 start-page: 105 year: 2008 ident: B37 article-title: Homology modeling of hemagglutinin/protease [HA/P (vibriolysin)] from Vibrio cholerae: sequence comparision, residue interactions and molecular mechanism. publication-title: Protein J. doi: 10.1007/s10930-007-9113-0 contributor: fullname: Lutfullah – volume: 18 start-page: 3425 year: 2016 ident: B50 article-title: Phenotype and toxicity of the recently discovered exlA-positive Pseudomonas aeruginosa strains collected worldwide. publication-title: Environ. Microbiol. doi: 10.1111/1462-2920.13262 contributor: fullname: Reboud – volume: 304 start-page: 990 year: 2014 ident: B57 article-title: Virulence attributes in brazilian clinical isolates of Pseudomonas aeruginosa. publication-title: Int. J. Med. Microbiol. doi: 10.1016/j.ijmm.2014.07.001 contributor: fullname: Silva – volume: 40 start-page: 277 year: 2015 ident: B72 article-title: The antibiotic resistance crisis - part 1: causes and threats. publication-title: PT. contributor: fullname: Ventola – volume: 64 start-page: 37 year: 1996 ident: B67 article-title: Contribution of specific Pseudomonas aeruginosa virulence factors to pathogenesis of pneumonia in a neonatal mouse model of infection. publication-title: Infect. Immun. doi: 10.1128/IAI.64.1.37-43.1996 contributor: fullname: Tang – volume: 30 start-page: 345 year: 2013 ident: B5 article-title: Diverse susceptibility of Galleria mellonella humoral immune response factors to the exoproteinase activity of entomopathogenic and clinical strains of Pseudomonas aeruginosa. publication-title: Zool. Sci. doi: 10.2108/zsj.30.345 contributor: fullname: Andrejko – volume: 24 start-page: 350 year: 2018 ident: B8 article-title: Updates on the pathogenicity status of Pseudomonas aeruginosa. publication-title: Drug Discov. Today doi: 10.1016/j.drudis.2018.07.003 contributor: fullname: Azam – volume: 10 start-page: 1491 year: 2008 ident: B30 article-title: A novel secreted protease from Pseudomonas aeruginosa activates NF-kappaB through protease-activated receptors. publication-title: Cell Microbiol. doi: 10.1111/j.1462-5822.2008.01142.x contributor: fullname: Kida – volume: 77 year: 1999 ident: B24 article-title: PC SPARTAN Pro molecular modeling for desktop. publication-title: Chem. Eng. News doi: 10.1021/cen-v077n017.p002 contributor: fullname: Hehre – volume: 44 start-page: 1495 year: 2016 ident: B53 article-title: international nosocomial infection control consortium report, data summary of 50 countries for 2010-2015: device-associated module. publication-title: Am. J. Infect. Control. doi: 10.1016/j.ajic.2016.08.007 contributor: fullname: Rosenthal – volume: 148 start-page: 1061 year: 1993 ident: B54 article-title: Erythromycin inhibits the production of elastase by Pseudomonas aeruginosa without affecting its proliferation in vitro. publication-title: Am. Rev. Respir. Dis doi: 10.1164/ajrccm/148.4_pt_1.1061 contributor: fullname: Sakata – volume: 9 year: 2014 ident: B42 article-title: Evaluation of reference genes for gene expression analysis using quantitative RT-PCR in Azospirillum brasilense. publication-title: PLoS One. doi: 10.1371/journal.pone.0098162 contributor: fullname: McMillan – volume: 54 start-page: 32 year: 2014 ident: B23 article-title: The role of N-glycosylation sites in the activity, stability, and expression of the recombinant elastase expressed by Pichia pastoris. publication-title: Enzyme Microb. Technol. doi: 10.1016/j.enzmictec.2013.09.014 contributor: fullname: Han – volume: 58 start-page: 1133 year: 2009 ident: B63 article-title: Pseudomonas aeruginosa - a phenomenon of bacterial resistance. publication-title: J. Med. Microbiol. doi: 10.1099/jmm.0.009142-0 contributor: fullname: Strateva – volume: 529 start-page: 336 year: 2016 ident: B11 article-title: Antibacterial drug discovery in the resistance era. publication-title: Nature doi: 10.1038/nature17042 contributor: fullname: Brown – volume: 17 start-page: 635 year: 2004 ident: B39 article-title: Synthesis and X-ray crystal structure of [Ag(phendio)2]ClO4 (phendio = 1,10-phenanthroline-5,6-dione) and its effects on fungal and mammalian cells. publication-title: Biometals doi: 10.1007/s10534-004-1229-5 contributor: fullname: McCann – volume: 6 start-page: e1603 year: 2015 ident: B46 article-title: Intrinsic antimicrobial resistance determinants in the superbug Pseudomonas aeruginosa. publication-title: MBio doi: 10.1128/mBio.01603-15 contributor: fullname: Murray – volume: 4 year: 2018 ident: B1 article-title: Antimicrobial resistance mechanisms and potential synthetic treatments. publication-title: Future Sci. OA. doi: 10.4155/fsoa-2017-0109 contributor: fullname: Ali – volume: 12 start-page: 300 year: 2014 ident: B4 article-title: Targeting virulence: can we make evolution-proof drugs? publication-title: Nat. Rev. Microbiol. doi: 10.1038/nrmicro3232 contributor: fullname: Allen – volume: 149 start-page: 2291 year: 2003 ident: B14 article-title: Mutation of lasA and lasB reduces Pseudomonas aeruginosa invasion of epithelial cells. publication-title: Microbiology doi: 10.1099/mic.0.26280-0 contributor: fullname: Cowell – volume: 29 start-page: 949 year: 2013 ident: B26 article-title: Doxycycline interferes with quorum sensing-mediated virulence factors and biofilm formation in gram-negative bacteria. publication-title: World J. Microbiol. Biotechnol. doi: 10.1007/s11274-013-1252-1 contributor: fullname: Husain – volume: 18 start-page: 318 year: 2018 ident: B65 article-title: WHO pathogens priority list working group. discovery, research, and development of new antibiotics: the WHO priority list of antibiotic-resistant bacteria and tuberculosis. publication-title: Lancet. Infect. Dis. doi: 10.1016/S1473-3099(17)30753-3 contributor: fullname: Tacconelli – volume: 193 start-page: 265 year: 1951 ident: B36 article-title: Protein measurement with the folin phenol reagent. publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)52451-6 contributor: fullname: Lowry – volume: 19 year: 2018 ident: B60 article-title: Theoretical studies applied to the evaluation of the DFPase Bioremediation potential against chemical warfare agents intoxication. publication-title: Int. J. Mol. Sci. doi: 10.3390/ijms19041257 contributor: fullname: Soares – volume: 11 start-page: 371 year: 2013 ident: B35 article-title: Antimicrobial activity of metals: mechanisms, molecular targets and applications. publication-title: Nat. Rev. Microbiol. doi: 10.1038/nrmicro3028 contributor: fullname: Lemire – volume: 115 start-page: 14 year: 2014 ident: B6 article-title: Diverse effects of Galleria mellonella infection with entomopathogenic and clinical strains of Pseudomonas aeruginosa. publication-title: J. Invertebr. Pathol. doi: 10.1016/j.jip.2013.10.006 contributor: fullname: Andrejko – volume: 2 year: 2013 ident: B31 article-title: EVpedia: an integrated database of high-throughput data for systemic analyses of extracellular vesicles. publication-title: J. Extracell. Vesicles doi: 10.3402/jev.v2i0.20384 contributor: fullname: Kim – volume: 8 year: 2017 ident: B22 article-title: 1,10-Phenanthroline-5,6-dione-based compounds are effective in disturbing crucial physiological events of Phialophora verrucosa. publication-title: Front. Microbiol. doi: 10.3389/fmicb.2017.00076 contributor: fullname: Granato – volume: 24 start-page: 3958 year: 2015 ident: B58 article-title: Molecular insight into the inhibition mechanism of plant and rat 4-hydroxyphenylpyruvate dioxygenase by molecular docking and DFT calculations. publication-title: Med. Chem. Res. doi: 10.1007/s00044-015-1436-3 contributor: fullname: Silva – volume: 3 start-page: 668 year: 2012 ident: B19 article-title: 3-Hydroxy-1-alkyl-2-methylpyridine-4(1H) thiones: inhibition of the Pseudomonas aeruginosa virulence factor LasB. publication-title: ACS Med. Chem. Lett. doi: 10.1021/ml300128f contributor: fullname: Garner – volume: 8 year: 2017 ident: B18 article-title: Antifungal potential of copper(II), manganese(II) and silver(I) 1,10-phenanthroline chelates against multidrug-resistant fungal species forming the Candida haemulonii complex: impact on the planktonic and biofilm lifestyles. publication-title: Front. Microbiol. doi: 10.3389/fmicb.2017.01257 contributor: fullname: Gandra – volume: 121 start-page: 602 year: 2017 ident: B52 article-title: Analysis of multiple components involved in the interaction between Cryptococcus neoformans and Acanthamoeba castellanii. publication-title: Fungal Biol. doi: 10.1016/j.funbio.2017.04.002 contributor: fullname: Rizzo – volume: 65 start-page: 684 year: 2010 ident: B3 article-title: Attenuation of Pseudomonas aeruginosa virulence factors and biofilms by co-encapsulation of bismuth-ethanedithiol with tobramycin in liposomes. publication-title: J. Antimicrob. Chemother. doi: 10.1093/jac/dkq036 contributor: fullname: Alipour – volume: 4 year: 2018 ident: B28 article-title: The use of Galleria mellonella larvae to identify novel antimicrobial agents against fungal species of medical interest. publication-title: J. Fungi. doi: 10.3390/jof4030113 contributor: fullname: Kavanagh – volume: 55 start-page: 2670 year: 2011 ident: B13 article-title: Novel inhibitors of the Pseudomonas aeruginosa virulence factor LasB: a potential therapeutic approach for the attenuation of virulence mechanisms in pseudomonal infection. publication-title: Antimicrob. Agents Chemother. doi: 10.1128/AAC.00776-10 contributor: fullname: Cathcart – volume: 406 start-page: 959 year: 2000 ident: B62 article-title: Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen. publication-title: Nature doi: 10.1038/35023079 contributor: fullname: Stover – volume: 12 start-page: 1 year: 2018 ident: B51 article-title: Anti-Trichomonas vaginalis activity of 1,10-phenanthroline-5,6-dione-based metallodrugs and synergistic effect with metronidazole. publication-title: Parasitology. doi: 10.1017/S003118201800152X contributor: fullname: Rigo – volume: 12 start-page: 6059 year: 2017 ident: B2 article-title: Synthesized zinc peroxide nanoparticles (ZnO2-NPs): a novel antimicrobial, anti-elastase, anti-keratinase, and anti-inflammatory approach toward polymicrobial burn wounds. publication-title: Int. J. Nanomedicine doi: 10.2147/IJN.S141201 contributor: fullname: Ali – volume: 41 start-page: 1 year: 2013 ident: B9 article-title: A dynamic and intricate regulatory network determines Pseudomonas aeruginosa virulence. publication-title: Nucleic Acids Res. doi: 10.1093/nar/gks1039 contributor: fullname: Balasubramanian – volume: 7 year: 2017 ident: B16 article-title: A reliable assay to evaluate the virulence of Aspergillus nidulans using the alternative animal model Galleria mellonella (Lepidoptera). publication-title: Bio. Protocol. doi: 10.21769/BioProtoc.2329 contributor: fullname: Fernandes – volume: 9 year: 2019 ident: B27 article-title: Virulence characteristics and an action mode of antibiotic resistance in multidrug-resistant Pseudomonas aeruginosa. publication-title: Sci. Rep. doi: 10.1038/s41598-018-37422-9 contributor: fullname: Hwang – volume: 96 start-page: 2408 year: 1999 ident: B66 article-title: Pseudomonas aeruginosa killing of Caenorhabditis elegans used to identify P. aeruginosa virulence factors. publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.96.5.2408 contributor: fullname: Tan – volume: 128 start-page: 1 year: 2017 ident: B64 article-title: Anti-Pseudomonas aeruginosa IgG antibodies and chronic airway infection in bronchiectasis. publication-title: Respir. Med. doi: 10.1016/j.rmed.2017.05.001 contributor: fullname: Suarez-Cuartin – volume: 15 year: 2014 ident: B47 article-title: Pseudomonas aeruginosa elastase causes transient disruption of tight junctions and downregulation of PAR-2 in human nasal epithelial cells. publication-title: Respir. Res doi: 10.1186/1465-9921-15-21 contributor: fullname: Nomura – volume: 4 year: 2018 ident: B48 article-title: Recent advances in the use of Galleria mellonella model to study immune responses against human pathogens. publication-title: J. Fungi. doi: 10.3390/jof4040128 contributor: fullname: Pereira – volume: 266 start-page: 2864 year: 1991 ident: B68 article-title: Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-A resolution. publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)49927-9 contributor: fullname: Thayer – volume: 54 start-page: 4582 year: 2010 ident: B7 article-title: Efficacy of calcium-EDTA as an inhibitor for metallo-β-lactamase in a mouse model of Pseudomonas aeruginosa pneumonia. publication-title: Antimicrob. Agents Chemother. doi: 10.1128/AAC.00511-10 contributor: fullname: Aoki – volume: 6 year: 2011 ident: B33 article-title: Pseudomonas aeruginosa elastase provides an escape from phagocytosis by degrading the pulmonary surfactant protein-A. publication-title: PLoS One doi: 10.1371/journal.pone.0027091 contributor: fullname: Kuang – volume: 5 year: 2015 ident: B75 article-title: Mechanistic insights into elastin degradation by pseudolysin, the major virulence factor of the opportunistic pathogen Pseudomonas aeruginosa. publication-title: Sci. Rep. doi: 10.1038/srep09936 contributor: fullname: Yang – volume: 49 start-page: 3315 year: 2006 ident: B69 article-title: MolDock: a new technique for high-accuracy molecular docking. publication-title: J. Med. Chem. doi: 10.1021/jm051197e contributor: fullname: Thomsen – volume: 32 start-page: 301 year: 2014 ident: B21 article-title: Reactivation steps by 2-PAM of tabun-inhibited human acetylcholinesterase: reducing the computational cost in hybrid QM/MM methods. publication-title: J. Biomol. Struct. Dyn. doi: 10.1080/07391102.2013.765361 contributor: fullname: Goncalves – volume: 11 year: 2013 ident: B71 article-title: The Aeromonas salmonicida subsp. salmonicida exoproteome: global analysis, moonlighting proteins and putative antigens for vaccination against furunculosis. publication-title: Proteome. Sci. doi: 10.1186/1477-5956-11-44 contributor: fullname: Vanden Bergh – volume: 1 start-page: 47 ident: B41 article-title: In vitro and in vivo studies into the biological activities of 1,10-phenanthroline, 1,10-phenanthroline-5, 6-dione and its copper(II) and silver(I) complexes. publication-title: Toxicol. Res. doi: 10.1039/c2tx00010e contributor: fullname: McCann |
SSID | ssj0000402000 |
Score | 2.459342 |
Snippet | Elastase B (lasB) is a multifunctional metalloenzyme secreted by the gram-negative pathogen
, and this enzyme orchestrates several physiopathological events... Elastase B (lasB) is a multifunctional metalloenzyme secreted by the gram-negative pathogen Pseudomonas aeruginosa , and this enzyme orchestrates several... Elastase B (lasB) is a multifunctional metalloenzyme secreted by the gram-negative pathogen Pseudomonas aeruginosa, and this enzyme orchestrates several... |
SourceID | doaj pubmedcentral proquest crossref pubmed |
SourceType | Open Website Open Access Repository Aggregation Database Index Database |
StartPage | 1701 |
SubjectTerms | 1,10-phenanthroline-5,6-dione anti-virulence therapy elastase B metal-based compounds Microbiology Pseudomonas aeruginosa theoretical calculations |
SummonAdditionalLinks | – databaseName: Directory of Open Access Journals dbid: DOA link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV3PaxQxFA5SELyI9efWKhE8WGh0NpNkEm9d21JFpYdWegv52Z3LrOzsHPr_-If6XmZbdkXw4mUGkhkS8r0k3yMv3yPkbe1ME5RxLImomDA6MS2cZk4IyVMVTC7and--q7NL8eVKXm2k-sKYsFEeeBy4D1H6CA5cUD5ORZRggTlWGXh0E6MOclx9K77hTJU1GN2iqhrPJcELMwBTGzyGcpn3KBkz3dqHilz_3zjmn6GSG3vP6SPycE0a6dHY2V1yL3WPyf0xjeTNE_LruO0dxrRc0_M-DXEBpuV66tJyuG67Re_oj3Y5lNtF1N9QoHz0czdvfYsH7PSo3Gygi0ynh7Bans8TxsbMSzafxOShYseoZsRmsN9FiusHZmLqP9ITIN4rKKQz-u6r62cHFBulKEGwea2LXpRg86fk8vTk4tMZW2dfYEEovmLGScdhM0fQokwhNVpq48F9SlwFx6MTPsPbeJ2B-_Kstalccpo3yYvg6mdkp4PuvSDUe6-gOgNVCMLUyilVRZ0NmIIW8JyQg1ss7M9RZMOCc4K42YKbRdxswW1CZgjW3Xcoj10KwGjs2mjsv4xmQt7cQm1hOuEZievSYugtr2tldA0saEKej9DfNVWjOl2l4O9myyi2-rJd07XzItmtlAYmpfb-R-dfkgc4HCUKke-TndVySK-AGa386zIJfgM6Hw7p priority: 102 providerName: Directory of Open Access Journals – databaseName: Scholars Portal Journals: Open Access dbid: M48 link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV3fa9swEBajY7CXse5n1m5osIcVquLIsiwVxmjWlm6sow_NyJuRLDkxFHuzY2j-n_2hvZPdrhl52YuDf8VOvpPuO3T3HSEfYqPTXGrDvHCSCa08U8IoZoRIuI9yXQTtzvMf8mwqvs2S2d_y6OEPbDeGdthPatpcHVz_Xn2GAf8JI07wt4BAmVvM0tIHqAYDsdBDDn4RE7zOB7If5mUMlUJNylhKXA7gs37dcuOXrPmpIOe_iYP-m0p5zzedPiVPBlJJj3or2CYPfPWMPOrbTK6ekz_HZWsw52VOL1rfuRpMz7TU-Kabl1XdGvqzbLpQfUTtigIlpF-rRWlLXICnR6HygdYFHe_DbHqx8Jg7swjdfjxL9iU7RrUjNgF_6CjOL9ipqT2kJ0DMl3CQTujH76ad7FF8KEWJgvtlX_QyJKO_INPTk8svZ2zozsByIfmSaZMYDs4eQXWJz32qEqUthFeey9xwZ4Qt4FNbVQA35oVSOjLeKJ56K3ITvyRbFbzea0KttRJOF0AlcqFjaaSMnCo0mIoSsB2RvVsssl-9CEcGwQvilgXcMsQtC7iNyATBursO5bPDgbqZZ8NozFxinY7ASK0bC5fAtFa4qIDgLHVO5Qkfkfe3UGcw3HANxVS-7tqMx7HUKgaWNCKveujvHhWjel0k4e50zSjW3mX9TFUugqS3lAqYlnzzHz90hzzGnZCMyHfJ1rLp_FsgSEv7Ltj9DfEDD3A priority: 102 providerName: Scholars Portal |
Title | Disarming Pseudomonas aeruginosa Virulence by the Inhibitory Action of 1,10-Phenanthroline-5,6-Dione-Based Compounds: Elastase B (LasB) as a Chemotherapeutic Target |
URI | https://www.ncbi.nlm.nih.gov/pubmed/31428062 https://search.proquest.com/docview/2336983129 https://pubmed.ncbi.nlm.nih.gov/PMC6688126 https://doaj.org/article/d5bd907c6bd14d5183fd0f1747dd8c52 |
Volume | 10 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1La9tAEF6SQKGX0vSpPsIWemggcuTVarXbW5xH01IXH5Lim9iXbEEiBcs65P_kh3ZmZQe79NTLCiQLLf5GOzPab74h5HOqVW6F0rHnTsRcSR9LrmWsOc-YT6wqg3bn-Je4vOY_ptl0h2TrWphA2remGtQ3t4O6mgdu5d2tPV7zxI4n41MhpMTKl12yC-53I0UPyy9mREnSb0lCAqYAocoaZHGpAarFYHOYFIXGEsG2vFEQ7f9XpPk3YXLDA108J89WoSM96ae4T3Z8_YI86ZtJ3r8kD2dVq5HZMqOT1neuAQPTLdV-0c2qumk1_V0tulBjRM09hcCPfq_nlalwm52ehPoG2pR0eARr5mTukSEzDz19fJwdifgMNY3iEXg9R3EVwX5M7Vd6DuH3Ek7SEf3yU7ejQ4oPpShEsFncRa8C5fwVub44vzq9jFc9GGLLBVvGSmeagUtH6Fzmrc9lJpWBJMozYTVzmpsSjsrIEiJgVkqpEu21ZLk33Or0NdmrYXpvCTXGCLhcQsBguUqFFiJxslRgEJLDGJHDNRbFXS-1UUCKghAWAcICISwChBEZIViPv0OR7HCiWcyKlakULjMOcn8rjBtyl8HiVbqkhBQsd07ajEXk0xrqAl4q3CnRtW-6tmBpKpRMIRaKyJse-sdHrU0nIvmWUWzNZfsK2HEQ7l7Z7bv_vvM9eYr_QSAgsg9kb7no_EcIipbmIHxMgPHbdAjjmMuD8Fr8AYEqEa0 |
link.rule.ids | 230,314,727,780,784,864,885,2102,24318,27924,27925,53791,53793 |
linkProvider | National Library of Medicine |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3JbtswECXSFEV7KbqmTjcW6KEBIkemSIrsLc4Cp7UDH5wiN4GbbAGJHFj2If_TD-0MbQd20VMvEkBKEKE3JGfAN28I-ZoZnTupTRK4lwnXKiSKG5UYzgULqdNl1O4cXMreFf9xLa53iFjnwkTSvrNVu765bdfVJHIr727d0ZondjQcnEipFGa-PCKPRZbrzkaQHhdgjInSdHkoCSGYBowqZ5HHpduoF4PlYTKUGksl29qPomz_v3zNvymTG3vQ-QvyfOU80uPlIF-SnVC_Ik-W5STvX5Pfp1VjkNsypsMmLPwUTMw01ITZYlzV08bQX9VsEbOMqL2n4PrRi3pS2QoP2ulxzHCg05J2DmHVHE4CcmQmsapPSMShTE5R1Sjpwr7nKa4jWJGp-U7PwAGfQyPt0m9903QPKH6UohTBZnoXHUXS-RtydX42OuklqyoMieOSzRNthGGwqSN4XgQXciWUthBGBSadYd5wW8JdW1WCD8xKpXRqglEsD5Y7k70luzUM7x2h1loJ3SW4DI7rTBopU69KDSahOFxb5GCNRXG3FNsoIEhBCIsIYYEQFhHCFukiWA_PoUx2bJjOxsXKWAovrIfo30nrO9wLWL5Kn5YQhOXeKydYi3xZQ13AtMKzElOH6aIpWJZJrTLwhlpkbwn9w6fWptMi-ZZRbI1luwcsOUp3ryx3_7_f_Eye9kaDftG_uPz5njzD_xHpiOwD2Z3PFuEjuEhz-ylOiD-7UxJC |
linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3LbtswECTaFC16Cfqu0hcL9NAAka1QFEX2FscxkjYJfEiK3AS-ZAtoZMOyDvmffmh3KTuwi556kQBRggjNiNwFh7OEfEm1yq1QOvbciZgr6WPJtYw15xnziVVl8O68uBSn1_z7TXazUeoriPatqXr1r9teXU2DtnJ-a_trnVh_fHEshJS482Xuyv5D8ihLgWQbiXoYhDEvSpJuYRLSMAU4Vdaglkv10DMGS8SkaDeWCLY1JwXr_n_Fm3_LJjfmodEzsrsKIOlR19Hn5IGvX5DHXUnJu5fk97BqNOpbJnTc-NbNgGa6odov2klVzxpNf1aLNuw0ouaOQvhHz-ppZSpcbKdHYZcDnZX08ABGzvHUo05mGir7-Dg7EPEQnY3iAcx9juJYglWZmm_0BILwJVykA_r1XDeDfYovpWhHsLnFi14F4fkrcj06uTo-jVeVGGLLBVvGSmeawcSOALrMW5_LTCoDqZRnwmrmNDclnJWRJcTBrJRSJdpryXJvuNXpa7JTQ_feEmqMEdBcQthguUqFFiJxslRAC8nhGJH9NRbFvDPcKCBRQQiLAGGBEBYBwogMEKz7-9AqO1yYLSbFijCFy4xTCRDSuEPuMhjCSpeUkIjlzkmbsYh8XkNdwK-F6yW69rO2KViaCiVTiIgi8qaD_v5Va-pEJN8ixVZftluAzcG-e8Xevf9-8hN5Mh6OivOzyx_vyFP8HEGRyN6TneWi9R8gSlqaj-F_-AOa8RNV |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Disarming+Pseudomonas+aeruginosa+Virulence+by+the+Inhibitory+Action+of+1%2C10-Phenanthroline-5%2C6-Dione-Based+Compounds%3A+Elastase+B+%28LasB%29+as+a+Chemotherapeutic+Target&rft.jtitle=Frontiers+in+microbiology&rft.au=Galdino%2C+Anna+Clara+M.&rft.au=Viganor%2C+L%C3%ADvia&rft.au=de+Castro%2C+Alexandre+A.&rft.au=da+Cunha%2C+Elaine+F.+F.&rft.date=2019-08-02&rft.issn=1664-302X&rft.eissn=1664-302X&rft.volume=10&rft_id=info:doi/10.3389%2Ffmicb.2019.01701&rft.externalDBID=n%2Fa&rft.externalDocID=10_3389_fmicb_2019_01701 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1664-302X&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1664-302X&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1664-302X&client=summon |