AlmG, responsible for polymyxin resistance in pandemic Vibrio cholerae , is a glycyltransferase distantly related to lipid A late acyltransferases

The Journal of Biological Chemistry
Jeremy C HendersonM Stephen Trent

Abstract

Cationic antimicrobial peptides (CAMPs), such as polymyxins, are used as a last-line defense in treatment of many bacterial infections. However, some bacteria have developed resistance mechanisms to survive these compounds. Current pandemic O1 Vibrio cholerae biotype El Tor is resistant to polymyxins, whereas a previous pandemic strain of the biotype Classical is polymyxin-sensitive. The almEFG operon found in El Tor V. cholerae confers >100-fold resistance to antimicrobial peptides through aminoacylation of lipopolysaccharide (LPS), expected to decrease the negatively charged surface of the V. cholerae outer membrane. This Gram-negative system bears striking resemblance to a related Gram-positive cell-wall remodeling strategy that also promotes CAMP resistance. Mutants defective in AlmEF-dependent LPS modification exhibit reduced fitness in vivo Here, we present investigation of AlmG, the hitherto uncharacterized member of the AlmEFG pathway. Evidence for AlmG glycyl to lipid substrate transferase activity is demonstrated in vivo by heterologous expression of V. cholerae pathway enzymes in a specially engineered Escherichia coli strain. Development of a minimal keto-deoxyoctulosonate (Kdo)-lipid A domain in E. coli was necessa...Continue Reading

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Citations

Dec 24, 2017·The Journal of Biological Chemistry·Jose A Bengoechea
Jan 17, 2019·FEMS Microbiology Reviews·Flaviana Di LorenzoAntonio Molinaro
Nov 13, 2019·Journal of Bacteriology·Natasha A Bencivenga-BarryAndrew L Goodman
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Feb 26, 2019·Frontiers in Microbiology·Jessica Saul-McBeth, Jyl S Matson
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Jan 12, 2020·Communications Biology·Huimin ZhangYoujun Feng
Aug 21, 2021·Frontiers in Cardiovascular Medicine·Xinyi ShenZhongqun Wang

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