Biogenesis of bacterial membrane vesicles

被引：223

作者：

Deatherage, Brooke L. ^{[1
]}

Lara, J. Cano ^{[1
]}

Bergsbaken, Tessa ^{[1
]}

Barrett, Sara L. Rassoulian ^{[2
]}

Lara, Stephanie ^{[3
]}

Cookson, Brad T. ^{[1
,2
]}

机构：

[1] Univ Washington, Dept Microbiol, Seattle, WA 98195 USA

[2] Univ Washington, Dept Lab Med, Seattle, WA 98195 USA

[3] Univ Washington, Dept Pathol, Seattle, WA 98195 USA

来源：

MOLECULAR MICROBIOLOGY | 2009年 / 72卷 / 06期

基金：

美国国家卫生研究院;

关键词：

PEPTIDOGLYCAN-ASSOCIATED PROTEINS; PENICILLIN-BINDING PROTEIN-3; GROWING ESCHERICHIA-COLI; GRAM-NEGATIVE BACTERIA; CD4(+) T-CELLS; OUTER-MEMBRANE; PSEUDOMONAS-AERUGINOSA; SALMONELLA-TYPHIMURIUM; NEISSERIA-MENINGITIDIS; HELICOBACTER-PYLORI;

D O I：

10.1111/j.1365-2958.2009.06731.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

P>Membrane vesicle (MV) release remains undefined, despite its conservation among replicating Gram-negative bacteria both in vitro and in vivo. Proteins identified in Salmonella MVs, derived from the envelope, control MV production via specific defined domains that promote outer membrane protein-peptidoglycan (OM-PG) and OM protein-inner membrane protein (OM-PG-IM) interactions within the envelope structure. Modulation of OM-PG and OM-PG-IM interactions along the cell body and at division septa, respectively, maintains membrane integrity while co-ordinating localized release of MVs with distinct size distribution and protein content. These data support a model of MV biogenesis, wherein bacterial growth and division invoke temporary, localized reductions in the density of OM-PG and OM-PG-IM associations within the envelope structure, thus releasing OM as MVs.

引用

页码：1395 / 1407

页数：13

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