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* Department of Pediatrics, Harvard Medical School, and Gastrointestinal Cell Biology Laboratory, Children’s Hospital, Boston, MA 02115;
Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, CA 90095; and
Division of Immunology and Allergy, Hôpital Orthopédique, Lausanne, Switzerland
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 C
1 and C2
are required for IgA adherence to mouse Peyer’s patch M cells. This
distinguishes the M cell IgA receptor from CD89 (FcI), which binds
domains C2-C3. 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.
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