Document Detail


PcpA of Streptococcus pneumoniae mediates adherence to nasopharyngeal and lung epithelial cells and elicits functional antibodies in humans.
MedLine Citation:
PMID:  22796387     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Streptococcus pneumoniae (pneumococci) adhere to human nasopharyngeal (NP) epithelial cells as a first step in colonization and adherence of pneumococci to lung epithelia may be required to establish pneumonia. We sought to determine if PcpA can serve as an adhesin to human NP (D562) and lung (A549) epithelial cells and whether PcpA mediated adherence can be inhibited by human anti-PcpA antibodies. A PcpA isogenic mutant was constructed in a pneumococcal TIGR4 background. When the mutant and wild type strains were compared for their adherence to D562 and A549 cell lines, a reduction in adherence by the mutant was observed (p = 0.0001 for both cell types). PcpA was ectopically expressed on the surface of minimally-adherent heterologous host Escherichia coli resulting in augmented adherence to D562 (p = 0.002) and A549 (p = 0.015) cells. Total IgG was purified from a pool of 6 human sera having high IgG titers of anti-pneumococcal proteins. The purified IgG reduced TIGR4 adherence to D562 cells but we determined that this effect was largely due to bacterial cell aggregation as determined by flow cytometry and confocal microscopy. Fab fragments were prepared from pooled IgG sera. Inhibition of TIGR4 adherence to D562 cells was observed using the Fab fragments without causing bacterial aggregation (p = 0.0001). Depletion of PcpA-specific Fab fragments resulted in an increase in adherence of TIGR4 to D562 cells (p = 0.028). We conclude that PcpA can mediate adherence of pneumococci to human NP and lung epithelial cells and PcpA mediated adherence can be inhibited by human anti-PcpA antibodies.
Authors:
M Nadeem Khan; Sharad K Sharma; Laura M Filkins; Michael E Pichichero
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Publication Detail:
Type:  Journal Article     Date:  2012-07-14
Journal Detail:
Title:  Microbes and infection / Institut Pasteur     Volume:  14     ISSN:  1769-714X     ISO Abbreviation:  Microbes Infect.     Publication Date:  2012 Oct 
Date Detail:
Created Date:  2012-09-18     Completed Date:  2013-01-28     Revised Date:  2013-10-17    
Medline Journal Info:
Nlm Unique ID:  100883508     Medline TA:  Microbes Infect     Country:  France    
Other Details:
Languages:  eng     Pagination:  1102-10     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 Institut Pasteur. Published by Elsevier Masson SAS. All rights reserved.
Affiliation:
Center for Infectious Diseases and Vaccine Immunology, Research Institute, Rochester General Hospital, Rochester, NY 14621, USA.
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MeSH Terms
Descriptor/Qualifier:
Adhesins, Bacterial / genetics,  immunology,  metabolism*
Adult
Antibodies, Bacterial / blood*
Bacterial Adhesion*
Bacterial Proteins / genetics,  immunology,  metabolism*
Carrier Proteins / genetics,  immunology,  metabolism*
Cell Line
Epithelial Cells / microbiology*
Gene Deletion
Humans
Immunoglobulin G / blood
Streptococcus pneumoniae / immunology,  pathogenicity*
Virulence Factors / genetics,  immunology,  metabolism*
Grant Support
ID/Acronym/Agency:
R01 DC008671/DC/NIDCD NIH HHS
Chemical
Reg. No./Substance:
0/Adhesins, Bacterial; 0/Antibodies, Bacterial; 0/Bacterial Proteins; 0/Carrier Proteins; 0/Immunoglobulin G; 0/PcpA protein, Streptococcus; 0/Virulence Factors
Comments/Corrections

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


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