The human polymeric immunoglobulin receptor binds to Streptococcus pneumoniae via domains 3 and 4.

Détails

ID Serval
serval:BIB_6A9386BC2CFF
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
The human polymeric immunoglobulin receptor binds to Streptococcus pneumoniae via domains 3 and 4.
Périodique
Journal of Biological Chemistry
Auteur(s)
Lu L., Lamm M.E., Li H., Corthesy B., Zhang J.R.
ISSN
0021-9258
Statut éditorial
Publié
Date de publication
2003
Peer-reviewed
Oui
Volume
278
Numéro
48
Pages
48178-48187
Langue
anglais
Notes
Publication types: Journal Article
Résumé
Streptococcus pneumoniae (the pneumococcus) is a major cause of bacterial pneumonia, middle ear infection (otitis media), sepsis, and meningitis. Our previous study demonstrated that the choline-binding protein A (CbpA) of S. pneumoniae binds to the human polymeric immunoglobulin receptor (pIgR) and enhances pneumococcal adhesion to and invasion of cultured epithelial cells. In this study, we sought to determine the CbpA-binding motif on pIgR by deletional analysis. The extra-cellular portion of pIgR consists of five Ig-like domains (D1-D5), each of which contains 104-114 amino acids and two disulfide bonds. Deletional analysis of human pIgR revealed that the lack of either D3 or D4 resulted in the loss of CbpA binding, whereas complete deletions of domains D1, D2, and D5 had undetectable impacts. Subsequent analysis showed that domains D3 and D4 together were necessary and sufficient for the ligand-binding activity. Furthermore, CbpA binding of pIgR did not appear to require Ca2+ or Mg2+. Finally, treating pIgR with a reducing agent abolished CbpA binding, suggesting that disulfide bonding is required for the formation of CbpA-binding motif(s). These results strongly suggest a conformational CbpA-binding motif(s) in the D3/D4 region of human pIgR, which is functionally separated from the IgA-binding site(s).
Mots-clé
Amino Acid Motifs, Amino Acid Sequence, Animals, Bacterial Proteins, Binding Sites, COS Cells, Calcium/metabolism, DNA, Complementary/metabolism, DNA-Binding Proteins/chemistry, DNA-Binding Proteins/metabolism, Disulfides, Dithiothreitol/pharmacology, Dogs, Dose-Response Relationship, Drug, Edetic Acid/pharmacology, Egtazic Acid/pharmacology, Electrophoresis, Polyacrylamide Gel, Enzyme-Linked Immunosorbent Assay, Gene Deletion, Heat-Shock Proteins/chemistry, Heat-Shock Proteins/metabolism, Humans, Immunoblotting, Ligands, Magnesium/chemistry, Magnesium/metabolism, Mice, Models, Genetic, Models, Molecular, Molecular Sequence Data, Oligonucleotides/chemistry, Protein Binding, Protein Conformation, Protein Structure, Tertiary, Receptors, Polymeric Immunoglobulin/chemistry, Sequence Homology, Amino Acid, Streptococcus pneumoniae/metabolism
Pubmed
Web of science
Open Access
Oui
Création de la notice
25/01/2008 14:53
Dernière modification de la notice
20/08/2019 14:25
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