The beta-glucan-binding lectin site of mouse CR3 (CD11b/CD18) and its function in generating a primed state of the receptor that mediates cytotoxic activation in response to iC3b-opsonized target cells

Mouse leukocyte CR3 (Mac-1, alphaMbeta2 integrin) was shown to function as a receptor for beta-glucans in the same way as human CR3. Soluble zymosan polysaccharide (SZP) or pure beta-glucans labeled with FITC or 125I bound in a saturable and reversible manner to neutrophils, macrophages, and NK cell...

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Bibliographic Details
Published in:The Journal of immunology (1950) 1999-02, Vol.162 (4), p.2281-2290
Main Authors: Xia, Y, Vetvicka, V, Yan, J, Hanikýrová, M, Mayadas, T, Ross, G D
Format: Article
Language:English
Subjects:
Animals
Binding Sites - immunology
CD18 Antigens - immunology
CD18 Antigens - metabolism
Complement C3b - immunology
Complement C3b - metabolism
Cytotoxicity Tests, Immunologic
Cytotoxicity, Immunologic - immunology
Female
Glucans - immunology
Glucans - metabolism
Killer Cells, Natural - immunology
Kinetics
Lectins - immunology
Lectins - metabolism
Leukemia P388
Lymphocyte Activation - immunology
Macrophage-1 Antigen - genetics
Macrophage-1 Antigen - immunology
Macrophage-1 Antigen - metabolism
Macrophages, Peritoneal - immunology
Macrophages, Peritoneal - metabolism
Mice
Mice, Inbred BALB C
Mice, Inbred Strains
Mice, Knockout
Neutrophils - immunology
Neutrophils - metabolism
Opsonin Proteins - metabolism
Phagocytosis - immunology
Receptors, Immunologic - immunology
Receptors, Immunologic - metabolism
Solubility
Zymosan - immunology
Zymosan - metabolism
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Summary:Mouse leukocyte CR3 (Mac-1, alphaMbeta2 integrin) was shown to function as a receptor for beta-glucans in the same way as human CR3. Soluble zymosan polysaccharide (SZP) or pure beta-glucans labeled with FITC or 125I bound in a saturable and reversible manner to neutrophils, macrophages, and NK cells. This lectin activity was blocked by anti-CD11b mAb M1/70 or 5C6 and did not occur with leukocytes from CR3-/- (CD11b-deficient) mice. SZP preparations containing primarily mannose or glucose bound to CR3, and the binding of 125I-labeled beta-glucan to CR3 was competitively inhibited by beta-glucans from barley or seaweed, but not by yeast alpha-mannan. Also, as with human CR3, the lectin site of mouse CR3 was inhibited by alpha- or beta-methylglucoside (but not D-glucose), alpha- or beta-methylmannoside, and N-acetyl-D-glucosamine. Phagocytosis of zymosan and serum-opsonized zymosan was partially inhibited by anti-CR3 and was reduced to
ISSN:0022-1767
1550-6606
DOI:10.4049/jimmunol.162.4.2281