Sub-inhibitory cefsulodin sensitization of E. coli to β-lactams is mediated by PBP1b inhibition.

The combination of antibiotics is one of the strategies to combat drug-resistant bacteria, though only a handful of such combinations are in use, such as the β-lactam combinations. In the present study, the efficacy of a specific sub-inhibitory concentration of cefsulodin with other β-lactams was ev...

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Autores principales:	Sujoy K Sarkar, Mouparna Dutta, Akash Kumar, Dhriti Mallik, Anindya S Ghosh
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/60d51a052e4e402d8ecdf0347ec6cca5
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spelling	oai:doaj.org-article:60d51a052e4e402d8ecdf0347ec6cca52021-11-18T08:09:55ZSub-inhibitory cefsulodin sensitization of E. coli to β-lactams is mediated by PBP1b inhibition.1932-620310.1371/journal.pone.0048598https://doaj.org/article/60d51a052e4e402d8ecdf0347ec6cca52012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23139798/?tool=EBIhttps://doaj.org/toc/1932-6203The combination of antibiotics is one of the strategies to combat drug-resistant bacteria, though only a handful of such combinations are in use, such as the β-lactam combinations. In the present study, the efficacy of a specific sub-inhibitory concentration of cefsulodin with other β-lactams was evaluated against a range of Gram-negative clinical isolates. This approach increased the sensitivity of the isolates, regardless of the β-lactamase production. The preferred target and mechanism of action of cefsulodin were identified in laboratory strains of Escherichia coli, by examining the effects of deleting the penicillin-binding protein (PBP) 1a and 1b encoding genes individually. Deletion of PBP1b was involved in sensitizing the bacteria to β-lactam agents, irrespective of its O-antigen status. Moreover, the use of a sub-inhibitory concentration of cefsulodin in combination with a β-lactam exerted an effect similar to that one obtained for PBP1b gene deletion. We conclude that the identified β-lactam/cefsulodin combination works by inhibiting PBP1b (at least partially) despite the involvement of β-lactamases, and therefore could be extended to a broad range of Gram-negative pathogens.Sujoy K SarkarMouparna DuttaAkash KumarDhriti MallikAnindya S GhoshPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 11, p e48598 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Sujoy K Sarkar Mouparna Dutta Akash Kumar Dhriti Mallik Anindya S Ghosh Sub-inhibitory cefsulodin sensitization of E. coli to β-lactams is mediated by PBP1b inhibition.
description	The combination of antibiotics is one of the strategies to combat drug-resistant bacteria, though only a handful of such combinations are in use, such as the β-lactam combinations. In the present study, the efficacy of a specific sub-inhibitory concentration of cefsulodin with other β-lactams was evaluated against a range of Gram-negative clinical isolates. This approach increased the sensitivity of the isolates, regardless of the β-lactamase production. The preferred target and mechanism of action of cefsulodin were identified in laboratory strains of Escherichia coli, by examining the effects of deleting the penicillin-binding protein (PBP) 1a and 1b encoding genes individually. Deletion of PBP1b was involved in sensitizing the bacteria to β-lactam agents, irrespective of its O-antigen status. Moreover, the use of a sub-inhibitory concentration of cefsulodin in combination with a β-lactam exerted an effect similar to that one obtained for PBP1b gene deletion. We conclude that the identified β-lactam/cefsulodin combination works by inhibiting PBP1b (at least partially) despite the involvement of β-lactamases, and therefore could be extended to a broad range of Gram-negative pathogens.
format	article
author	Sujoy K Sarkar Mouparna Dutta Akash Kumar Dhriti Mallik Anindya S Ghosh
author_facet	Sujoy K Sarkar Mouparna Dutta Akash Kumar Dhriti Mallik Anindya S Ghosh
author_sort	Sujoy K Sarkar
title	Sub-inhibitory cefsulodin sensitization of E. coli to β-lactams is mediated by PBP1b inhibition.
title_short	Sub-inhibitory cefsulodin sensitization of E. coli to β-lactams is mediated by PBP1b inhibition.
title_full	Sub-inhibitory cefsulodin sensitization of E. coli to β-lactams is mediated by PBP1b inhibition.
title_fullStr	Sub-inhibitory cefsulodin sensitization of E. coli to β-lactams is mediated by PBP1b inhibition.
title_full_unstemmed	Sub-inhibitory cefsulodin sensitization of E. coli to β-lactams is mediated by PBP1b inhibition.
title_sort	sub-inhibitory cefsulodin sensitization of e. coli to β-lactams is mediated by pbp1b inhibition.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/60d51a052e4e402d8ecdf0347ec6cca5
work_keys_str_mv	AT sujoyksarkar subinhibitorycefsulodinsensitizationofecolitoblactamsismediatedbypbp1binhibition AT mouparnadutta subinhibitorycefsulodinsensitizationofecolitoblactamsismediatedbypbp1binhibition AT akashkumar subinhibitorycefsulodinsensitizationofecolitoblactamsismediatedbypbp1binhibition AT dhritimallik subinhibitorycefsulodinsensitizationofecolitoblactamsismediatedbypbp1binhibition AT anindyasghosh subinhibitorycefsulodinsensitizationofecolitoblactamsismediatedbypbp1binhibition
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Sub-inhibitory cefsulodin sensitization of E. coli to β-lactams is mediated by PBP1b inhibition.

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