Journal
MOLECULAR MICROBIOLOGY
Volume 72, Issue 6, Pages 1395-1407Publisher
WILEY
DOI: 10.1111/j.1365-2958.2009.06731.x
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Funding
- National Institutes of Health [AI47242, AI0055396]
- National Institute of General Medical Sciences Public Health Service National Research Service Award [T32 G07270]
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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.
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