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Altered lipid composition in Streptococcus pneumoniae cpoA mutants
BACKGROUND: Penicillin-resistance in Streptococcus pneumoniae is mainly due to alterations in genes encoding the target enzymes for beta-lactams, the penicillin-binding proteins (PBPs). However, non-PBP genes are altered in beta-lactam-resistant laboratory mutants and confer decreased susceptibility...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3901891/ https://www.ncbi.nlm.nih.gov/pubmed/24443834 http://dx.doi.org/10.1186/1471-2180-14-12 |
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author | Meiers, Marina Volz, Carsten Eisel, Jessica Maurer, Patrick Henrich, Bernhard Hakenbeck, Regine |
author_facet | Meiers, Marina Volz, Carsten Eisel, Jessica Maurer, Patrick Henrich, Bernhard Hakenbeck, Regine |
author_sort | Meiers, Marina |
collection | PubMed |
description | BACKGROUND: Penicillin-resistance in Streptococcus pneumoniae is mainly due to alterations in genes encoding the target enzymes for beta-lactams, the penicillin-binding proteins (PBPs). However, non-PBP genes are altered in beta-lactam-resistant laboratory mutants and confer decreased susceptibility to beta-lactam antibiotics. Two piperacillin resistant laboratory mutants of Streptococcus pneumoniae R6 contain mutations in the putative glycosyltransferase gene cpoA. The CpoA gene is part of an operon including another putative glycosyltransferase gene spr0982, both of which being homologous to glycolipid synthases present in other Gram-positive bacteria. RESULTS: We now show that the cpoA mutants as well as a cpoA deletion mutant are defective in the synthesis of galactosyl-glucosyl-diacylglycerol (GalGlcDAG) in vivo consistent with the in vitro function of CpoA as α-GalGlcDAG synthase as shown previously. In addition, the proportion of phosphatidylglycerol increased relative to cardiolipin in cpoA mutants. Moreover, cpoA mutants are more susceptible to acidic stress, have an increased requirement for Mg(2+) at low pH, reveal a higher resistance to lysis inducing conditions and are hypersensitive to bacitracin. CONCLUSIONS: The data show that deficiency of the major glycolipid GalGlcDAG causes a pleitotropic phenotype of cpoA mutant cells consistent with severe membrane alterations. We suggest that the cpoA mutations selected with piperacillin are directed against the lytic response induced by the beta-lactam antibiotic. |
format | Online Article Text |
id | pubmed-3901891 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-39018912014-01-26 Altered lipid composition in Streptococcus pneumoniae cpoA mutants Meiers, Marina Volz, Carsten Eisel, Jessica Maurer, Patrick Henrich, Bernhard Hakenbeck, Regine BMC Microbiol Research Article BACKGROUND: Penicillin-resistance in Streptococcus pneumoniae is mainly due to alterations in genes encoding the target enzymes for beta-lactams, the penicillin-binding proteins (PBPs). However, non-PBP genes are altered in beta-lactam-resistant laboratory mutants and confer decreased susceptibility to beta-lactam antibiotics. Two piperacillin resistant laboratory mutants of Streptococcus pneumoniae R6 contain mutations in the putative glycosyltransferase gene cpoA. The CpoA gene is part of an operon including another putative glycosyltransferase gene spr0982, both of which being homologous to glycolipid synthases present in other Gram-positive bacteria. RESULTS: We now show that the cpoA mutants as well as a cpoA deletion mutant are defective in the synthesis of galactosyl-glucosyl-diacylglycerol (GalGlcDAG) in vivo consistent with the in vitro function of CpoA as α-GalGlcDAG synthase as shown previously. In addition, the proportion of phosphatidylglycerol increased relative to cardiolipin in cpoA mutants. Moreover, cpoA mutants are more susceptible to acidic stress, have an increased requirement for Mg(2+) at low pH, reveal a higher resistance to lysis inducing conditions and are hypersensitive to bacitracin. CONCLUSIONS: The data show that deficiency of the major glycolipid GalGlcDAG causes a pleitotropic phenotype of cpoA mutant cells consistent with severe membrane alterations. We suggest that the cpoA mutations selected with piperacillin are directed against the lytic response induced by the beta-lactam antibiotic. BioMed Central 2014-01-20 /pmc/articles/PMC3901891/ /pubmed/24443834 http://dx.doi.org/10.1186/1471-2180-14-12 Text en Copyright © 2014 Meiers et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Article Meiers, Marina Volz, Carsten Eisel, Jessica Maurer, Patrick Henrich, Bernhard Hakenbeck, Regine Altered lipid composition in Streptococcus pneumoniae cpoA mutants |
title | Altered lipid composition in Streptococcus pneumoniae cpoA mutants |
title_full | Altered lipid composition in Streptococcus pneumoniae cpoA mutants |
title_fullStr | Altered lipid composition in Streptococcus pneumoniae cpoA mutants |
title_full_unstemmed | Altered lipid composition in Streptococcus pneumoniae cpoA mutants |
title_short | Altered lipid composition in Streptococcus pneumoniae cpoA mutants |
title_sort | altered lipid composition in streptococcus pneumoniae cpoa mutants |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3901891/ https://www.ncbi.nlm.nih.gov/pubmed/24443834 http://dx.doi.org/10.1186/1471-2180-14-12 |
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