Document Detail


Plasminogen- and fibronectin-binding protein B is involved in the adherence of Streptococcus pneumoniae to human epithelial cells.
MedLine Citation:
PMID:  20048164     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Salvatore Papasergi; Manuela Garibaldi; Giovanna Tuscano; Giacomo Signorino; Susanna Ricci; Samuele Peppoloni; Ida Pernice; Carla Lo Passo; Giuseppe Teti; Franco Felici; Concetta Beninati
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-01-04
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  285     ISSN:  1083-351X     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2010 Mar 
Date Detail:
Created Date:  2010-03-01     Completed Date:  2010-04-29     Revised Date:  2011-07-26    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  7517-24     Citation Subset:  IM    
Affiliation:
Elie Metchnikoff Department, Università di Messina, Messina I-98125, Italy.
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MeSH Terms
Descriptor/Qualifier:
Adhesins, Bacterial / genetics,  metabolism*
Amino Acid Sequence
Animals
Bacterial Adhesion / physiology*
Bacterial Proteins / metabolism*
Carrier Proteins / metabolism*
Cell Line
Epithelial Cells / cytology,  microbiology*
Fibronectins / metabolism*
Humans
Mice
Microspheres
Molecular Sequence Data
Open Reading Frames
Plasminogen / metabolism*
Pneumococcal Infections / metabolism
Protein Binding
Recombinant Fusion Proteins / genetics,  metabolism
Streptococcus pneumoniae / metabolism*
Chemical
Reg. No./Substance:
0/Adhesins, Bacterial; 0/Bacterial Proteins; 0/Carrier Proteins; 0/Fibronectins; 0/PfbB protein, Streptococcus pneumoniae; 0/Recombinant Fusion Proteins; 9001-91-6/Plasminogen
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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