Proteomics in Gram-negative bacterial outer membrane vesicles.
SCIE
SCOPUS
- Title
- Proteomics in Gram-negative bacterial outer membrane vesicles.
- Authors
- Lee, EY; Choi, DS; Kim, KP; Gho, YS
- Date Issued
- 2008-11
- Publisher
- Wiley Subscription Services, Inc.
- Abstract
- Gram-negative bacteria constitutively secrete outer membrane vesicles (OMVs) into the extracellular milieu. Recent research in this area has revealed that OMVs may act as intercellular communicasomes in polyspecies communities by enhancing bacterial survival and pathogenesis in hosts. However, the mechanisms of vesicle formation and the pathophysiological roles of OMVs have not been clearly defines. While it is obvious that mass spectrometry-based proteomics offers great opportunities for improving our knowledge of bacterial OMVs limited proteomic data are available for OMVs. The present review aim to give an overviews of the previous biochemical, biological, and proteomic studies in the emerging field of bacterial OMVs, and to give future directions for high- throughput and comparative proteomic studies of OMVs that originate from diverse Gram-negative bacteria under various environmental conditions. This article will hopefully stimulate further efforts to construct a comprehensive proteome data-base of bacterial OMVs that will help us not only to develop the biogenesis and functions of OMVs but also to develop diagnostic tools, vaccine, and antibiotics effective against pathogenic bacteria. (C) 2008 Wiley Periodicals, Inc., Mass Spec Rev 27:535-555. 2008
- Keywords
- outer membrane vesicles; gram-negative bacteria; communicasomes; antibiotics; proteomics; vaccines; INDUCED FLUORESCENCE DETECTION; GENERAL SECRETORY PATHWAY; PROTEIN SUBCELLULAR-LOCALIZATION; FREE-FLOW ELECTROPHORESIS; GROWING ESCHERICHIA-COLI; HEAT-LABILE ENTEROTOXIN; PSEUDOMONAS-AERUGINOSA; MASS-SPECTROMETRY; NEISSERIA-MENINGITIDIS; CAPILLARY-ELECTROPHORESIS
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/29388
- DOI
- 10.1002/MAS.20175
- ISSN
- 0277-7037
- Article Type
- Article
- Citation
- MASS SPECTROMETRY REVIEWS, vol. 27, no. 6, page. 535 - 555, 2008-11
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