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Plasminogen- and fibronectin-binding protein B is involved in the adherence of Streptococcus pneumoniae to human epithelial cells.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 2010 Mar 05; Vol. 285 (10), pp. 7517-24. Date of Electronic Publication: 2010 Jan 04. - Publication Year :
- 2010
-
Abstract
- Streptococcus pneumoniae is a major cause of morbidity and mortality worldwide. The ability of this bacterium to adhere to epithelial cells is considered as an essential early step in colonization and infection. By screening a whole genome phage display library with sera from infected patients, we previously identified three antigenic fragments matching open reading frame spr0075 of the strain R6 genome. This locus encodes for an approximately 120-kDa protein, herein referred to as plasminogen- and fibronectin-binding protein B (PfbB), which displays an LPXTG cell wall anchoring motif and six repetitive domains. In this study, by using isogenic pfbB-deleted mutants of the encapsulated D39 and of the unencapsulated DP1004 type 2 pneumococcal strains, we show that PfbB is involved in S. pneumoniae adherence to various epithelial respiratory tract cell lines. Our data suggest that PfbB directly mediates bacterial adhesion, because fluorescent beads coated with the recombinant PfbB sp17 fragment (encompassing one of the six repetitive domains and the C-terminal region) efficiently bound to epithelial cells. Mutants lacking PfbB bound to fibronectin and plasminogen considerably less efficiently than wild type bacteria, whereas sp17-coated beads specifically bound to both of these substrates. Taken together, our data suggest that, by directly interacting with fibronectin, PfbB significantly increases the ability of S. pneumoniae to adhere to human epithelial cells.
- Subjects :
- Adhesins, Bacterial genetics
Amino Acid Sequence
Animals
Cell Line
Epithelial Cells cytology
Humans
Mice
Microspheres
Molecular Sequence Data
Open Reading Frames
Pneumococcal Infections metabolism
Protein Binding
Recombinant Fusion Proteins genetics
Recombinant Fusion Proteins metabolism
Adhesins, Bacterial metabolism
Bacterial Adhesion physiology
Bacterial Proteins metabolism
Carrier Proteins metabolism
Epithelial Cells microbiology
Fibronectins metabolism
Plasminogen metabolism
Streptococcus pneumoniae metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1083-351X
- Volume :
- 285
- Issue :
- 10
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 20048164
- Full Text :
- https://doi.org/10.1074/jbc.M109.062075