期刊论文详细信息
PLoS Pathogens
Vibrio cholerae ensures function of host proteins required for virulence through consumption of luminal methionine sulfoxide
Paula I. Watnick1  Adam CN Wong2  Vidhya Vijayakumar2  Audrey S. Vanhove2  Saiyu Hang2  John M. Asara3 
[1] Department of Medicine, Harvard Medical School, Boston MA, United States of America;Division of Infectious Diseases, Boston Children’s Hospital, Harvard Medical School, 300 Longwood Avenue, Boston MA, United States of America;Division of Signal Transduction, Beth Israel Deaconess Medical Center, 3 Blackfan Circle, Boston MA, United States of America
关键词: Vibrio cholerae;    Gastrointestinal tract;    Methionine;    Glycine;    Lipids;    Drosophila melanogaster;    Gastrointestinal infections;    Lipid analysis;   
DOI  :  10.1371/journal.ppat.1006428
学科分类:生物科学(综合)
来源: Public Library of Science
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【 摘 要 】

Vibrio cholerae is a diarrheal pathogen that induces accumulation of lipid droplets in enterocytes, leading to lethal infection of the model host Drosophila melanogaster. Through untargeted lipidomics, we provide evidence that this process is the product of a host phospholipid degradation cascade that induces lipid droplet coalescence in enterocytes. This infection-induced cascade is inhibited by mutation of the V. cholerae glycine cleavage system due to intestinal accumulation of methionine sulfoxide (MetO), and both dietary supplementation with MetO and enterocyte knock-down of host methionine sulfoxide reductase A (MsrA) yield increased resistance to infection. MsrA converts both free and protein-associated MetO to methionine. These findings support a model in which dietary MetO competitively inhibits repair of host proteins by MsrA. Bacterial virulence strategies depend on functional host proteins. We propose a novel virulence paradigm in which an intestinal pathogen ensures the repair of host proteins essential for pathogenesis through consumption of dietary MetO.

【 授权许可】

CC BY   

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