A D, D‐carboxypeptidase is required for Vibrio cholerae halotolerance. (February 2015)
- Record Type:
- Journal Article
- Title:
- A D, D‐carboxypeptidase is required for Vibrio cholerae halotolerance. (February 2015)
- Main Title:
- A D, D‐carboxypeptidase is required for Vibrio cholerae halotolerance
- Authors:
- Möll, Andrea
Dörr, Tobias
Alvarez, Laura
Davis, Brigid M.
Cava, Felipe
Waldor, Matthew K. - Abstract:
- <abstract abstract-type="main"> <title>Summary</title> <p>The biological roles of low molecular weight penicillin‐binding proteins (LMW PBP) have been difficult to discern in Gram‐negative organisms. In <italic>E</italic><italic>scherichia coli</italic>, mutants lacking these proteins often have no phenotype, and cells lacking all seven LMW PBPs remain viable. In contrast, we report here that <italic>V</italic><italic>ibrio cholerae</italic> lacking DacA‐1, a PBP5 homologue, displays slow growth, aberrant morphology and altered peptidoglycan (PG) homeostasis in Luria–Bertani (LB) medium, as well as a profound plating defect. DacA‐1 alone among <italic>V</italic><italic>. cholerae's</italic> LMW PBPs is critical for bacterial growth; mutants lacking the related protein DacA‐2 and/or homologues of PBP4 or PBP7 displayed normal growth and morphology. Remarkably, the growth and morphology of the <italic>dac</italic><italic>A</italic><italic>‐1</italic> mutant were unimpaired in LB media containing reduced concentrations of NaCl (100 mM or less), and also within suckling mice, a model host for the study of cholera pathogenesis. Peptidoglycan from the <italic>dac</italic><italic>A</italic><italic>‐1</italic> mutant contained elevated pentapeptide levels in standard and low salt media, and comparative analyses suggest that DacA‐1 is <italic>V</italic><italic>. cholerae's</italic> principal DD‐carboxypeptidase. The basis for the<abstract abstract-type="main"> <title>Summary</title> <p>The biological roles of low molecular weight penicillin‐binding proteins (LMW PBP) have been difficult to discern in Gram‐negative organisms. In <italic>E</italic><italic>scherichia coli</italic>, mutants lacking these proteins often have no phenotype, and cells lacking all seven LMW PBPs remain viable. In contrast, we report here that <italic>V</italic><italic>ibrio cholerae</italic> lacking DacA‐1, a PBP5 homologue, displays slow growth, aberrant morphology and altered peptidoglycan (PG) homeostasis in Luria–Bertani (LB) medium, as well as a profound plating defect. DacA‐1 alone among <italic>V</italic><italic>. cholerae's</italic> LMW PBPs is critical for bacterial growth; mutants lacking the related protein DacA‐2 and/or homologues of PBP4 or PBP7 displayed normal growth and morphology. Remarkably, the growth and morphology of the <italic>dac</italic><italic>A</italic><italic>‐1</italic> mutant were unimpaired in LB media containing reduced concentrations of NaCl (100 mM or less), and also within suckling mice, a model host for the study of cholera pathogenesis. Peptidoglycan from the <italic>dac</italic><italic>A</italic><italic>‐1</italic> mutant contained elevated pentapeptide levels in standard and low salt media, and comparative analyses suggest that DacA‐1 is <italic>V</italic><italic>. cholerae's</italic> principal DD‐carboxypeptidase. The basis for the <italic>dac</italic><italic>A</italic><italic>‐1</italic> mutant's halosensitivity is unknown; nonetheless, the mutant's survival in biochemically uncharacterized environments (such as the suckling mouse intestine) can be used as a reporter of low Na<sup>+</sup> content.</p> </abstract> … (more)
- Is Part Of:
- Environmental microbiology. Volume 17:Number 2(2015:Feb.)
- Journal:
- Environmental microbiology
- Issue:
- Volume 17:Number 2(2015:Feb.)
- Issue Display:
- Volume 17, Issue 2 (2015)
- Year:
- 2015
- Volume:
- 17
- Issue:
- 2
- Issue Sort Value:
- 2015-0017-0002-0000
- Page Start:
- 527
- Page End:
- 540
- Publication Date:
- 2015-02
- Subjects:
- Microbial ecology -- Periodicals
Environmental Microbiology -- Periodicals
579.17 - Journal URLs:
- http://firstsearch.oclc.org ↗
http://firstsearch.oclc.org/journal=1462-2912;screen=info;ECOIP ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1462-2920/issues ↗
http://www.blackwell-synergy.com/member/institutions/issuelist.asp?journal=emi ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/1462-2920.12779 ↗
- Languages:
- English
- ISSNs:
- 1462-2912
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3791.522600
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 3683.xml