Literature DB >> 18248419

Penicillin-binding proteins and beta-lactam resistance.

André Zapun1, Carlos Contreras-Martel, Thierry Vernet.   

Abstract

A number of ways and means have evolved to provide resistance to eubacteria challenged by beta-lactams. This review is focused on pathogens that resist by expressing low-affinity targets for these antibiotics, the penicillin-binding proteins (PBPs). Even within this narrow focus, a great variety of strategies have been uncovered such as the acquisition of an additional low-affinity PBP, the overexpression of an endogenous low-affinity PBP, the alteration of endogenous PBPs by point mutations or homologous recombination or a combination of the above.

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Year:  2008        PMID: 18248419     DOI: 10.1111/j.1574-6976.2007.00095.x

Source DB:  PubMed          Journal:  FEMS Microbiol Rev        ISSN: 0168-6445            Impact factor:   16.408


  178 in total

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8.  The structures of penicillin-binding protein 4 (PBP4) and PBP5 from Enterococci provide structural insights into β-lactam resistance.

Authors:  Thomas M Moon; Éverton D D'Andréa; Christopher W Lee; Alexei Soares; Jean Jakoncic; Charlene Desbonnet; Monica Garcia-Solache; Lou B Rice; Rebecca Page; Wolfgang Peti
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10.  Early insights into the interactions of different β-lactam antibiotics and β-lactamase inhibitors against soluble forms of Acinetobacter baumannii PBP1a and Acinetobacter sp. PBP3.

Authors:  Krisztina M Papp-Wallace; Baui Senkfor; Julian Gatta; Weirui Chai; Magdalena A Taracila; Veerabahu Shanmugasundaram; Seungil Han; Richard P Zaniewski; Brian M Lacey; Andrew P Tomaras; Marion J Skalweit; Michael E Harris; Louis B Rice; John D Buynak; Robert A Bonomo
Journal:  Antimicrob Agents Chemother       Date:  2012-08-20       Impact factor: 5.191

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