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

Journal Article · Mon May 01 00:00:00 EDT 1989 · J. Cell Biol.; (United States)

DOI:https://doi.org/10.1083/jcb.108.5.1673· OSTI ID:6080846

Weltzin, R; Lucia-Jandris, P; Michetti, P; Fields, B N; Kraehenbuhl, J P; Neutra, M R

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

• Research Organization: Harvard Univ. Medical School, Boston, MA (USA)
• OSTI ID: 6080846
• Journal Information: J. Cell Biol.; (United States), Journal Name: J. Cell Biol.; (United States) Vol. 108:5; ISSN JCLBA
• Country of Publication: United States
• Language: English

Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
ANIMAL CELLS
ANIMAL TISSUES
ANIMALS
ANTIBODIES
ANTIGEN-ANTIBODY REACTIONS
AUTORADIOGRAPHY
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BIOCHEMICAL REACTION KINETICS
BODY
CELL CONSTITUENTS
CELL MEMBRANES
COLLOIDS
DAYS LIVING RADIOISOTOPES
DIGESTIVE SYSTEM
DISPERSIONS
ELECTRON MICROSCOPY
EPITHELIUM
EVEN-ODD NUCLEI
FLUORESCENCE
GLANDS
GLOBULINS
HYBRIDOMAS
IMMUNOGLOBULINS
ISOTOPE APPLICATIONS
ISOTOPES
KINETICS
LIGHT NUCLEI
LIVER
LUMINESCENCE
MAMMALS
MEMBRANE PROTEINS
MEMBRANE TRANSPORT
MEMBRANES
MICE
MICROORGANISMS
MICROSCOPY
MOLECULAR WEIGHT
MONOCLONAL ANTIBODIES
NUCLEI
ONCOGENIC VIRUSES
ORGANIC COMPOUNDS
ORGANS
PARASITES
PROTEINS
RABBITS
RADIOISOTOPES
RATS
REACTION KINETICS
RECEPTORS
RODENTS
SPECIFICITY
SULFUR 35
SULFUR ISOTOPES
TISSUES
TRACER TECHNIQUES
VERTEBRATES
VIRUSES