Modulation of bacterial outer membrane vesicle production by envelope structure and content.

dc.contributor.author

Schwechheimer, Carmen

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Kulp, Adam

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Kuehn, Meta J

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England

dc.date.accessioned

2015-10-05T18:21:55Z

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2014-12-21

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BACKGROUND: Vesiculation is a ubiquitous secretion process of Gram-negative bacteria, where outer membrane vesicles (OMVs) are small spherical particles on the order of 50 to 250 nm composed of outer membrane (OM) and lumenal periplasmic content. Vesicle functions have been elucidated in some detail, showing their importance in virulence factor secretion, bacterial survival, and biofilm formation in pathogenesis. Furthermore, OMVs serve as an envelope stress response, protecting the secreting bacteria from internal protein misfolding stress, as well as external envelope stressors. Despite their important functional roles very little is known about the regulation and mechanism of vesicle production. Based on the envelope architecture and prior characterization of the hypervesiculation phenotypes for mutants lacking the lipoprotein, Lpp, which is involved in the covalent OM-peptidoglycan (PG) crosslinks, it is expected that an inverse relationship exists between OMV production and PG-crosslinked Lpp. RESULTS: In this study, we found that subtle modifications of PG remodeling and crosslinking modulate OMV production, inversely correlating with bound Lpp levels. However, this inverse relationship was not found in strains in which OMV production is driven by an increase in "periplasmic pressure" resulting from the accumulation of protein, PG fragments, or lipopolysaccharide. In addition, the characterization of an nlpA deletion in backgrounds lacking either Lpp- or OmpA-mediated envelope crosslinks demonstrated a novel role for NlpA in envelope architecture. CONCLUSIONS: From this work, we conclude that OMV production can be driven by distinct Lpp concentration-dependent and Lpp concentration-independent pathways.

dc.identifier

http://www.ncbi.nlm.nih.gov/pubmed/25528573

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s12866-014-0324-1

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1471-2180

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https://hdl.handle.net/10161/10654

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eng

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Springer Science and Business Media LLC

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BMC Microbiol

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10.1186/s12866-014-0324-1

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Bacterial Outer Membrane Proteins

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Cell Membrane

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Cell Wall

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Escherichia coli

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Escherichia coli Proteins

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Gene Deletion

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Lipoproteins

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Peptidoglycan

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Protein Binding

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Secretory Vesicles

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Modulation of bacterial outer membrane vesicle production by envelope structure and content.

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Journal article

pubs.author-url

http://www.ncbi.nlm.nih.gov/pubmed/25528573

pubs.begin-page

324

pubs.organisational-group

Basic Science Departments

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Biochemistry

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Duke

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Duke Cancer Institute

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Institutes and Centers

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Molecular Genetics and Microbiology

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School of Medicine

pubs.publication-status

Published online

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14

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