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Class A Penicillin-Binding Protein-Mediated Cell Wall Synthesis Promotes Structural Integrity during Peptidoglycan Endopeptidase Insufficiency in Vibrio cholerae

Shannon G. Murphy, Andrew N. Murtha, Ziyi Zhao, Laura Álvarez, Peter J Diebold, Jung‐Ho Shin, Michael S. VanNieuwenhze, Felipe Cava, Tobias Dörr

2021mBio23 citationsDOIOpen Access PDF

Abstract

, one class of turnover enzymes, the endopeptidases, are necessary for proper cell elongation and division. aPBPs become essential for maintaining structural integrity during EP insufficiency, while the Rod system remains active but contributes little to cell expansion under these conditions. Our results suggest that aPBPs are more versatile than the Rod system in their ability to recognize cell wall gaps formed by autolysins other than the major endopeptidases, adding to our understanding of the coordination between autolysins and cell wall synthases. A detailed understanding of autolysin biology may promote the development of antibiotics that target these essential turnover processes.

Topics & Concepts

PeptidoglycanAutolysinVibrio choleraeMreBCell wallPenicillin binding proteinsBacterial cell structureBiologyMicrobiologyCell biologyBiochemistryCellPenicillinBacteriaCytoskeletonAntibioticsGeneticsAntibiotic Resistance in BacteriaBacterial Genetics and BiotechnologyVibrio bacteria research studies
Class A Penicillin-Binding Protein-Mediated Cell Wall Synthesis Promotes Structural Integrity during Peptidoglycan Endopeptidase Insufficiency in Vibrio cholerae | Litcius