AN IC3B RECEPTOR ON CANDIDA-ALBICANS - STRUCTURE, FUNCTION, AND CORRELATES FOR PATHOGENICITY
AN IC3B RECEPTOR ON CANDIDA-ALBICANS - STRUCTURE, FUNCTION, AND CORRELATES FOR PATHOGENICITY
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DOI：
10.1093/infdis/157.1.38
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发表时间：
1988-01-01
影响因子：
6.4
通讯作者：
HOSTETTER, MK
中科院分区：
文献类型：
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作者：
GILMORE, BJ;RETSINAS, EM;HOSTETTER, MK
到目前为止，哺乳动物补体蛋白生物活性片段的膜受体的存在仅限于哺乳动物细胞，这些受体通过触发微生物入侵的吞噬反应的多个方面来保护宿主。在这项研究中，我们发现C3片段iC3b的表面受体存在于酵母白色念珠菌上，在那里它们通过抑制吞噬作用来促进该生物体的致病性。这些受体与α具有同源性。-链，但不带。beta。-链，中性粒细胞受体的iC3b，由单克隆抗体的结合决定，并由酵母的菌丝转化和高浓度葡萄糖诱导。单克隆抗体阻断这些受体可显著增强所研究菌株的吞噬能力。通过非共价结合iC3b，这些受体损害人类多形核白细胞对白色念珠菌的吞噬摄取。
Heretofore, the existence of membrane receptors for biologically active fragments of mammalian complement proteins has been confined to mammalian cells, where these receptors serve to protect the host by triggering multiple aspects of the phagocytic response to microbial invasion. In this study, we show that surface receptors for the C3 fragment iC3b are present on the yeast Candida albicans, where they promote the pathogenicity of this organism by inhibiting phagocytosis. These receptors share homology with the .alpha.-chain, but not with the .beta.-chain, of neutrophil receptors for iC3b, as determined by the binding of monoclonal antibodies, and are induced by mycelial transformation of the yeast and by high concentrations of glucose. Blockade of these receptors by monoclonal antibodies significantly augments phagocytosis for those strains studied. By binding iC3b noncovalently, these receptors impair phagocytic uptake of C. albicans by human polymorphonuclear leukocytes.