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tvi
ka*
ová*
*
Division of Experimental Immunology and Immunopathology, Department of Pathology, and
Department of Microbiology and Immunology, University of Louisville, Louisville, KY 40292; and
Department of Pathology, Harvard University, Boston, MA 02115
Mouse leukocyte CR3 (Mac-1, 
Mß2
integrin) was shown to function as a receptor for ß-glucans in the
same way as human CR3. Soluble zymosan polysaccharide (SZP) or pure
ß-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 ß-glucan to CR3 was
competitively inhibited by ß-glucans from barley or seaweed, but not
by yeast -mannan. Also, as with human CR3, the lectin site of mouse
CR3 was inhibited by - or ß-methylglucoside (but not
D-glucose), - or ß-methylmannoside, and
N-acetyl-D-glucosamine. Phagocytosis of
zymosan and serum-opsonized zymosan was partially inhibited by
anti-CR3 and was reduced to <40% of normal with leukocytes from
CR3-/- mice. As with neutrophils from patients with CD18
deficiency, neutrophils from CR3-/- mice exhibited no
phagocytosis of particulate ß-glucan. SZP or ß-glucans primed CR3
of neutrophils, macrophages, and NK cells for cytotoxicity of
iC3b-opsonized tumor cells that otherwise did not trigger killing.
ß-Glucan priming for cytotoxicity was inhibited by anti-CR3 and
did not occur with leukocytes from CR3-/- mice. The
primed state of macrophage and NK cell CR3 remained detectable for 18
to 24 h after pulsing with ß-glucans. The similarity of mouse
and human CR3 in response to ß-glucans highlights the utility of
mouse tumor models for development of therapeutic
ß-glucans.
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