Selective adherence of IgA to murine Peyer's patch M cells: evidence for a novel IgA receptor.

Details

Serval ID
serval:BIB_BBCB7008AA1F
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Selective adherence of IgA to murine Peyer's patch M cells: evidence for a novel IgA receptor.
Journal
Journal of Immunology
Author(s)
Mantis N.J., Cheung M.C., Chintalacharuvu K.R., Rey J., Corthésy B., Neutra M.R.
ISSN
0022-1767[print], 0022-1767[linking]
Publication state
Published
Issued date
2002
Volume
169
Number
4
Pages
1844-1851
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
Publication Status: ppublish
Abstract
M cells represent the primary route by which mucosal Ags are transported across the intestinal epithelium and delivered to underlying gut-associated lymphoid tissues. In rodents and rabbits, Peyer's patch M cells selectively bind and endocytose secretory IgA (SIgA) Abs. Neither the nature of the M cell IgR nor the domains of SIgA involved in this interaction are known. Using a mouse ligated ileal loop assay, we found that monoclonal IgA Abs with or without secretory component, but not IgG or IgM Abs, bound to the apical surfaces of Peyer's patch M cells, indicating that the receptor is specific for the IgA isotype. Human serum IgA and colostral SIgA also bound to mouse M cells. The asialoglycoprotein receptor or other lectin-like receptors were not detected on the apical surfaces of M cells. We used recombinant human IgA1 and human IgA2 Abs and domain swapped IgA/IgG chimeras to determine that both domains Calpha1 and Calpha2 are required for IgA adherence to mouse Peyer's patch M cells. This distinguishes the M cell IgA receptor from CD89 (FcalphaI), which binds domains Calpha2-Calpha3. Finally, we observed by immunofluorescence microscopy that some M cells in the human ileum are coated with IgA. Together these data suggest that mouse, and possibly human, M cells express an IgA-specific receptor on their apical surfaces that mediates the transepithelial transport of SIgA from the intestinal lumen to underlying gut-associated organized lymphoid tissues.
Keywords
Animals, Asialoglycoprotein Receptor, Binding Sites, Endocytosis, Female, Hepatocytes/immunology, Hepatocytes/metabolism, Humans, Immunity, Mucosal, Immunoglobulin A, Secretory/chemistry, Immunoglobulin A, Secretory/metabolism, Mice, Mice, Inbred BALB C, Mice, Knockout, Peyer's Patches/cytology, Peyer's Patches/immunology, Protein Structure, Tertiary, Rats, Rats, Sprague-Dawley, Receptors, Cell Surface/metabolism, Receptors, Fc/metabolism
Pubmed
Web of science
Create date
25/01/2008 14:53
Last modification date
20/08/2019 15:29
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