Binding and transepithelial transport of immunoglobulins by intestinal M cells: demonstration using monoclonal IgA antibodies against enteric viral proteins.

• DOI: 10.1083/jcb.108.5.1673
• Publication Date: 2004-05-15T00:18:20Z
• Authors: R Weltzin; P Lucia-Jandris; P Michetti; B N Fields; J P Kraehenbuhl; M R Neutra
• Keywords: Microfold cell; Secretory component; Immunoglobulin A; Isotype; Peyer's patch; Hapten

M cells of intestinal epithelia overlying lymphoid follicles endocytose luminal macromolecules and microorganisms deliver them to underlying tissue. The effect secretory IgA antibodies on adherence transepithelial transport antigens by is unknown. We have studied the interaction monoclonal directed against specific enteric viruses, or hapten trinitrophenyl (TNP), with cells. To produce monospecific mouse mammary tumor virus (MMTV) reovirus type 1, Peyer's patch from mucosally immunized mice were fused myeloma cells, generating hybridomas that secreted virus-specific in monomeric polymeric forms. One two anti-MMTV specifically bound viral surface glycoprotein gp52, 3 10 antireovirus immunoprecipitated sigma mu lc proteins. 35S-labeled injected intravenously into rats recovered bile as higher molecular weight species, suggesting component had been added passage through liver. Radiolabeled colloidal gold-conjugated was mouse, rat, rabbit loops containing patches. Light microscopic autoradiography EM showed all (antivirus anti-TNP) cell membranes transported vesicles across IgA-gold binding inhibited excess unlabeled IgA, indicating specific. IgG-gold also adhered IgG binding; thus not isotype-specific. Immune complexes consisting anti-TNP TNP-ferritin selectively membranes, while alone did not. These results suggest selective antibody may facilitate delivery virus-antibody mucosal tissue, enhancing subsequent immune responses facilitating invasion.