4.6 Article

Pbp, a cell-surface exposed plasminogen binding protein of Bacteroides fragilis

Journal

MICROBES AND INFECTION
Volume 10, Issue 5, Pages 514-521

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.micinf.2008.01.015

Keywords

plasminogen binding protein; peritonitis; bacterial synergy; Bacteroides fragilis; Escherichia coli; lipoprotein

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The Gram-negative anaerobic bacterium B. fragilis is a member of the commensal flora of the human intestine, but is also frequently found in severe intra-abdominal infections. Several B. fragilis virulence factors have been implicated in the development of these infections. A B.fragilis protein of circa 60-kDa was identified as a putative plasminogen binding protein (Pbp). The corresponding gene was located, cloned, sequenced and the subcellular localization of the protein was investigated. Pbp was both determined in the outer membrane of B. fragilis and of E. coli that expressed the cloned protein. Protease accessibility studies showed that the protein is expressed at the cell surface. Importantly, we demonstrated that Pbp is sufficient and required for plasminogen binding to whole cells in both E. coli and B. fragilis. Pbp-like proteins were also detected in some other Bacteroides subspecies. The role of this potential B. fragilis virulence factor in pathogenicity is discussed. (C) 2008 Elsevier Masson SAS. All rights reserved.

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