Abstract：
:Outer membrane vesicle formation occurs during Gram-negative bacterial growth. However, natural production of large amounts of outer membrane vesicles has only been described in a few bacterial genera. The purified vesicles of some bacterial pathogens have shown potential applications in vaccinology and in antibiotic therapy. This study focused on the development of a gene expression system able to induce production of large amounts of outer membrane vesicles. The Tol-Pal system of Escherichia coli, required to maintain outer membrane integrity, is composed of five cell envelope proteins, TolA, TolB, TolQ, TolR and Pal. Tol proteins are parasitized by filamentous bacteriophages and by colicins. The phage infection process and colicin import require, respectively, the N-terminal domain of the minor coat g3p protein and the translocation domain of colicins, with both domains interacting with Tol proteins. In this study, we show that the periplasmic production of either Tol, g3p or colicin domains was able to specifically destabilize the E. coli or Shigella flexneri cell envelope and to induce production of high amounts of vesicles. This technique was further found to work efficiently in Salmonella enterica serovar Typhimurium.
journal_name
Res Microbioljournal_title
Research in microbiologyauthors
Henry T,Pommier S,Journet L,Bernadac A,Gorvel JP,Lloubès Rdoi
10.1016/j.resmic.2004.04.007subject
Has Abstractpub_date
2004-07-01 00:00:00pages
437-46issue
6eissn
0923-2508issn
1769-7123pii
S0923-2508(04)00105-6journal_volume
155pub_type
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更新日期：2003-07-01 00:00:00
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journal_title：Research in microbiology
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journal_title：Research in microbiology
pub_type： 杂志文章
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更新日期：2014-09-01 00:00:00
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journal_title：Research in microbiology
pub_type： 杂志文章
doi：10.1016/j.resmic.2010.03.004
更新日期：2010-05-01 00:00:00
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journal_title：Research in microbiology
pub_type： 杂志文章,评审
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