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dc.contributor.author | Ropy, Alaa | - |
dc.contributor.author | Cabot, Gabriel | - |
dc.contributor.author | Sánchez-Diener, Irina | - |
dc.contributor.author | Aguilera, Cristina | - |
dc.contributor.author | Moyà, Bartolomé | - |
dc.contributor.author | Ayala, Juan Alfonso | - |
dc.contributor.author | Oliver, Antonio | - |
dc.date.accessioned | 2015-11-10T08:59:47Z | - |
dc.date.available | 2015-11-10T08:59:47Z | - |
dc.date.issued | 2015 | - |
dc.identifier | doi: 10.1128/AAC.05150-14 | - |
dc.identifier | issn: 1098-6596 | - |
dc.identifier.citation | Antimicrobial Agents and Chemotherapy 59(7): 3925-3934 (2015) | - |
dc.identifier.uri | http://hdl.handle.net/10261/124717 | - |
dc.description.abstract | This study aimed to characterize the role of Pseudomonas aeruginosa low-molecular-mass penicillin-binding proteins (LMM PBPs), namely, PBP4 (DacB), PBP5 (DacC), and PBP7 (PbpG), in peptidoglycan composition, β-lactam resistance, and ampC regulation. For this purpose, we constructed all single and multiple mutants of dacB, dacC, pbpG, and ampC from the wild-type P. aeruginosa PAO1 strain. Peptidoglycan composition was determined by high-performance liquid chromatography (HPLC), ampC expression by reverse transcription-PCR (RT-PCR), PBP patterns by a Bocillin FL-binding test, and antimicrobial susceptibility by MIC testing for a panel of β-lactams. Microscopy and growth rate analyses revealed no apparent major morphological changes for any of the mutants compared to the wild-type PAO1 strain. Of the single mutants, only dacC mutation led to significantly increased pentapeptide levels, showing that PBP5 is the major DD-carboxypeptidase in P. aeruginosa. Moreover, our results indicate that PBP4 and PBP7 play a significant role as DD-carboxypeptidase only if PBP5 is absent, and their DD-endopeptidase activity is also inferred. As expected, the inactivation of PBP4 led to a significant increase in ampC expression (around 50-fold), but, remarkably, the sequential inactivation of the three LMM PBPs produced a much greater increase (1,000-fold), which correlated with peptidoglycan pentapeptide levels. Finally, the β-lactam susceptibility profiles of the LMM PBP mutants correlated well with the ampC expression data. However, the inactivation of ampC in these mutants also evidenced a role of LMM PBPs, especially PBP5, in intrinsic β-lactam resistance. In summary, in addition to assessing the effect of P. aeruginosa LMM PBPs on peptidoglycan structure for the first time, we obtained results that represent a step forward in understanding the impact of these PBPs on β-lactam resistance, apparently driven by the interplay between their roles in AmpC induction, β-lactam trapping, and DD-carboxypeptidase/β-lactamase activity. | - |
dc.description.sponsorship | This work was supported by the Ministerio de Economía y Competitividad of Spain and the Instituto de Salud Carlos III through the Spanish Network for the Research in Infectious Diseases (grants RD06/0008 and RD12/0015) and grants PS09/00033 and PI12/00103. The work at CBMSO was supported by grants BFU2009-09200 from the Ministerio de Economía y Competitividad of Spain and 223431 DIVINOCELL from the European Union. We acknowledge the predoctoral grant JAE/Predoc from the Consejo Superior de Investigaciones Cientificas to A.R. The study is also supported by the Direcció General d’Universitats, Recerca i Transferència del Coneixement del Govern de les Illes Balears, Spain. | - |
dc.publisher | American Society for Microbiology | - |
dc.relation.isversionof | Publisher's version | - |
dc.rights | openAccess | - |
dc.title | Role of Pseudomonas aeruginosa low-molecular-mass penicillin-binding proteins in AmpC expression, β-lactam resistance, and peptidoglycan structure | - |
dc.type | artículo | - |
dc.identifier.doi | 10.1128/AAC.05150-14 | - |
dc.date.updated | 2015-11-10T08:59:48Z | - |
dc.description.version | Peer Reviewed | - |
dc.language.rfc3066 | eng | - |
dc.contributor.funder | Instituto de Salud Carlos III | - |
dc.contributor.funder | Consejo Superior de Investigaciones Científicas (España) | - |
dc.contributor.funder | Govern de les Illes Balears | - |
dc.contributor.funder | Ministerio de Economía y Competitividad (España) | - |
dc.relation.csic | Sí | - |
dc.identifier.funder | http://dx.doi.org/10.13039/501100004587 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/501100003339 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/501100003329 | es_ES |
dc.identifier.pmid | 25896695 | - |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.openairetype | artículo | - |
item.grantfulltext | open | - |
item.cerifentitytype | Publications | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.fulltext | With Fulltext | - |
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Ayala Juan A Role of Pseudomonas.pdf | 514,73 kB | Adobe PDF | Visualizar/Abrir |
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