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Specificity of membrane complement receptor type three (CR3) for beta-glucans.

G D Ross·J A Cain·B L Myones·S L Newman·P J Lachmann
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Abstract

The binding of the iC3b receptor (CR3) to unopsonized zymosan was shown to result from CR3 attachment to cell wall beta-glucans. A specificity of neutrophil responses for beta-glucan was first suggested by a comparison of yeast (Saccharomyces cerevisiae) cell wall components for stimulation of a neutrophil superoxide burst. Neutrophils responded poorly to heat-killed yeast, but gave increasingly better responses to cell wall polysaccharides devoid of proteins (zymosan) and nearly pure beta-glucan particles derived from zymosan. Zymosan triggered a burst that was 29% as great as that stimulated by phorbol myristate acetate (PMA), and beta-glucan particles stimulated a burst that was 72% as great as that produced by PMA. Phagocytic responses to yeast were also inhibited by soluble glucans but not by soluble mannans. Three types of experiments demonstrated a role for CR3 in these responses. First, neutrophil ingestion of either yeast or yeast-derived beta-glucan particles was blocked by monoclonal anti-CR3, fluid-phase iC3b, or soluble beta-glucan from barley. Monocyte ingestion of beta-glucan particles was also blocked by anti-CR3, but not by anti-CR1 or anti-C3. Second, the neutrophil superoxide burst response to either zymosan or beta-glucan particles was blocked by anti-CR3 or fluid-phase iC3b, and was completely absent with neutrophils from 3 patients with an inherited deficiency of CR3. Third, CR3 was isolated from solubilized neutrophils by affinity chromatography on beta-glucan-Sepharose.

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GlucansHumansImmunologic Deficiency SyndromesIn Vitro TechniquesMonocytesNeutrophilsPhagocytosisReceptors, Cell SurfaceReceptors, ComplementReceptors, Complement 3bReceptors, ImmunologicSaccharomyces cerevisiaeSuperoxidesZymosanJournal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, P.H.S.

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G D Ross, J A Cain, B L Myones, S L Newman, P J Lachmann. 1987. Specificity of membrane complement receptor type three (CR3) for beta-glucans.. https://doi.org/10.1159/000463010

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