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Secretory immunoglobulin A carries oligosaccharide receptors for Escherichia coli type 1 fimbrial lectin.

Artikel i vetenskaplig tidskrift
Författare Agnes E Wold
J Mestecky
M Tomana
A Kobata
H Ohbayashi
T Endo
C S Edén
Publicerad i Infection and immunity
Volym 58
Nummer/häfte 9
Sidor 3073-7
ISSN 0019-9567
Publiceringsår 1990
Publicerad vid
Sidor 3073-7
Språk en
Ämnesord Agglutination, drug effects, Carbohydrate Sequence, Escherichia coli, metabolism, Humans, Immunoglobulin A, Secretory, metabolism, Lectins, metabolism, Lectins, C-Type, Mannose-Binding Lectins, Molecular Sequence Data, Myeloma Proteins, pharmacology, Receptors, Cell Surface, Receptors, Fc, Receptors, Immunologic, metabolism, Tumor Cells, Cultured
Ämneskategorier Immunologi inom det medicinska området, Immunologi

Sammanfattning

Type 1 fimbriae with mannose-specific lectins are widely distributed among members of the family Enterobacteriaceae and confer the ability to attach to a range of host cells, including colonic epithelial cells. The mucosal surfaces are protected by secretory immunoglobulin A (IgA), which agglutinates microorganisms and prevents their attachment to host epithelial cells. This action has been attributed to a specificity of the antigen-combining site of mucosal immunoglobulins for bacterial and viral surface components. Here, we report a novel mechanism for the antibacterial effect of secretory IgA. Secretory IgA and IgA myeloma proteins, especially those of the IgA2 subclass, were shown to possess carbohydrate receptors for the mannose-specific lectin of type 1-fimbriated Escherichia coli. The presence of the high-mannose oligosaccharide chain Man alpha 1-6(Man alpha 1-3)Man alpha 1-6(Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4GlcNAc correlated with binding activity. The interaction between bacterial mannose-specific lectins and IgA receptor oligosaccharide resulted in agglutination of the bacteria and in inhibition of bacterial attachment to colonic epithelial cells. Thus, this interaction could form the basis for a broad antibacterial function of secretory IgA against enterobacteria regardless of the specificity of antibody molecules.

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