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

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...

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Bibliographic Details
Published in:Microbes and infection 2008-04, Vol.10 (5), p.514-521
Main Authors: Sijbrandi, Robert, Stork, Michiel, Luirink, Joen, Otto, Ben R.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacterial Outer Membrane Proteins - genetics
Bacterial Outer Membrane Proteins - isolation & purification
Bacterial Outer Membrane Proteins - metabolism
Bacterial Proteins - genetics
Bacterial Proteins - isolation & purification
Bacterial Proteins - metabolism
Bacterial synergy
Bacteriology
Bacteroides fragilis
Bacteroides fragilis - genetics
Bacteroides fragilis - metabolism
Biological and medical sciences
Blotting, Western
Carrier Proteins - genetics
Carrier Proteins - isolation & purification
Carrier Proteins - metabolism
Cloning, Molecular
Databases, Protein
Escherichia coli
Escherichia coli - metabolism
Fundamental and applied biological sciences. Psychology
Gene Expression
Genes, Bacterial
Genetic Vectors
Humans
Lipoprotein
Microbiology
Miscellaneous
Peritonitis
Plasmids
Plasminogen - metabolism
Plasminogen binding protein
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Summary: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.
ISSN:1286-4579
1769-714X
DOI:10.1016/j.micinf.2008.01.015