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Septal Class A Penicillin-Binding Protein Activity and <scp>ld</scp> -Transpeptidases Mediate Selection of Colistin-Resistant Lipooligosaccharide-Deficient Acinetobacter baumannii

Katie N. Kang, Misha I. Kazi, Jacob Biboy, Joe Gray, Hannah Bovermann, Jessie Ausman, Cara C. Boutte, Waldemar Vollmer, Joseph M. Boll

2021mBio31 citationsDOIOpen Access PDF

Abstract

The increasing prevalence of antibiotic treatment failure associated with Gram-negative bacterial infections highlights an urgent need to develop new alternative therapeutic strategies. The last-line antimicrobial colistin (polymyxin E) targets the ubiquitous outer membrane lipopolysaccharide (LPS)/LOS membrane anchor, lipid A, which is essential for viability of most diderms.

Topics & Concepts

Acinetobacter baumanniiColistinMicrobiologyPeptidoglycanBacterial outer membraneGlycosyltransferasePenicillin binding proteinsCell wallBiologyAntibioticsBacteriaGenePenicillinEscherichia coliPseudomonas aeruginosaBiochemistryGeneticsAntibiotic Resistance in BacteriaBacterial Genetics and BiotechnologyBacterial biofilms and quorum sensing
Septal Class A Penicillin-Binding Protein Activity and <scp>ld</scp> -Transpeptidases Mediate Selection of Colistin-Resistant Lipooligosaccharide-Deficient Acinetobacter baumannii | Litcius