SIgA Binding to Mucosal Surfaces Is Mediated by Mucin-Mucin Interactions

Gibbins, Hannah L., Proctor, Gordon B., Yakubov, Gleb E., Wilson, Stephen and Carpenter, Guy H. (2015) SIgA Binding to Mucosal Surfaces Is Mediated by Mucin-Mucin Interactions. PLoS One, 10 3: e0126887-e0126887. doi:10.1371/journal.pone.0119677


Author Gibbins, Hannah L.
Proctor, Gordon B.
Yakubov, Gleb E.
Wilson, Stephen
Carpenter, Guy H.
Title SIgA Binding to Mucosal Surfaces Is Mediated by Mucin-Mucin Interactions
Journal name PLoS One   Check publisher's open access policy
ISSN 1932-6203
Publication date 2015-03-20
Year available 2015
Sub-type Article (original research)
DOI 10.1371/journal.pone.0119677
Open Access Status DOI
Volume 10
Issue 3
Start page e0126887
End page e0126887
Total pages 13
Place of publication San Francisco, CA United States
Publisher Public Library of Science
Language eng
Subject 2700 Medicine
1300 Biochemistry, Genetics and Molecular Biology
1100 Agricultural and Biological Sciences
Abstract The oral mucosal pellicle is a layer of absorbed salivary proteins, including secretory IgA (SIgA), bound onto the surface of oral epithelial cells and is a useful model for all mucosal surfaces. The mechanism by which SIgA concentrates on mucosal surfaces is examined here using a tissue culture model with real saliva. Salivary mucins may initiate the formation of the mucosal pellicle through interactions with membrane-bound mucins on cells. Further protein interactions with mucins may then trigger binding of other pellicle proteins. HT29 colon cell lines, which when treated with methotrexate (HT29-MTX) produce a gel-forming mucin, were used to determine the importance of these mucin-mucin interactions. Binding of SIgA to cells was then compared using whole mouth saliva, parotid (mucin-free) saliva and a source of purified SIgA. Greatest SIgA binding occurred when WMS was incubated with HT29-MTX expressing mucus. Since salivary MUC5B was only able to bind to cells which produced mucus and purified SIgA showed little binding to the same cells we conclude that most SIgA binding to mucosal cells occurs because SIgA forms complexes with salivary mucins which then bind to cells expressing membrane-bound mucins. This work highlights the importance of mucin interactions in the development of the mucosal pellicle.
Formatted abstract
The oral mucosal pellicle is a layer of absorbed salivary proteins, including secretory IgA (SIgA), bound onto the surface of oral epithelial cells and is a useful model for all mucosal surfaces. The mechanism by which SIgA concentrates on mucosal surfaces is examined here using a tissue culture model with real saliva. Salivary mucins may initiate the formation of the mucosal pellicle through interactions with membrane-bound mucins on cells. Further  protein interactions with mucins may then trigger binding of other pellicle proteins. HT29 colon cell lines, which when treated with methotrexate (HT29-MTX) produce a gel-forming mucin, were used to determine the importance of these mucin-mucin interactions. Binding of SIgA to cells was then compared using whole mouth saliva, parotid (mucin-free) saliva and a source of purified SIgA. Greatest SIgA binding occurred when WMS was incubated with HT29-MTX expressing mucus. Since salivary MUC5B was only able to bind to cells which produced mucus and purified SIgA showed little binding to the same cells we conclude that most SIgA binding to mucosal cells occurs because SIgA forms complexes with salivary mucins which then bind to cells expressing membrane-bound mucins. This work highlights the importance of mucin interactions in the development of the mucosal pellicle.  
Keyword Mucin
Mucus
Saliva
Cell Binding
Cell membranes
Structural Proteins
Q-Index Code C1
Q-Index Status Confirmed Code
Grant ID BB/F01827/1
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: School of Chemical Engineering Publications
Official 2016 Collection
 
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Created: Tue, 24 Mar 2015, 21:44:33 EST by Gleb Yakubov on behalf of School of Chemical Engineering