Related Experiment Video
Updated: Jul 6, 2026

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
Published on: December 17, 2013
Pbp, a cell-surface exposed plasminogen binding protein of Bacteroides fragilis
Robert Sijbrandi1, Michiel Stork, Joen Luirink
1Department of Molecular Microbiology, Faculty of Earth and Life Sciences, VU-University Amsterdam de Boelelaan 1085, 1081 HV Amsterdam, The Netherlands.
Abstract:
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.
Insights
Bacteroides fragilis plasminogen binding protein (Pbp) is a cell surface protein crucial for plasminogen binding. This protein is implicated as a virulence factor in intra-abdominal infections caused by B. fragilis.
Area of Science:
- Microbiology
- Bacterial Pathogenesis
- Molecular Biology
Background:
- Bacteroides fragilis, a Gram-negative anaerobic bacterium, resides in the human gut but is linked to severe intra-abdominal infections.
- Virulence factors of B. fragilis are key to its role in infection development.
Purpose of the Study:
- To identify and characterize a putative plasminogen binding protein (Pbp) from B. fragilis.
- To investigate the role of Pbp in plasminogen binding and its potential contribution to pathogenicity.
Main Methods:
- Gene cloning, sequencing, and protein expression in E. coli.
- Subcellular localization studies using protease accessibility assays.
- Assessment of Pbp's necessity and sufficiency for plasminogen binding.
Main Results:
- A ~60-kDa protein, Pbp, was identified and localized to the outer membrane and cell surface of B. fragilis.
- Pbp was sufficient and necessary for plasminogen binding to whole bacterial cells.
- Pbp-like proteins were found in other Bacteroides subspecies.
Conclusions:
- The cell surface protein Pbp plays a significant role in B. fragilis-mediated plasminogen binding.
- Pbp is a potential virulence factor contributing to the pathogenicity of B. fragilis infections.
Related Concept Videos
Regulation of Bacterial Virulence
Formation of Lipopolysaccharides
Determinants of Bacterial Pathogenicity and Virulence
Bacterial Translocation and Protein Secretion
Inhibitors of Gram-positive Cell Wall Synthesis
Bacterial Phylum Proteobacteria

