BINDING OF CRYPTOCOCCUS-NEOFORMANS BY HUMAN CULTURED MACROPHAGES - REQUIREMENTS FOR MULTIPLE COMPLEMENT RECEPTORS AND ACTIN

被引:94
作者
LEVITZ, SM [1 ]
TABUNI, A [1 ]
机构
[1] BOSTON UNIV HOSP, MED CTR, DEPT MED, BOSTON, MA 02118 USA
关键词
CRYPTOCOCCOSIS; DIVALENT CATIONS; FUNGUS; PHAGOCYTOSIS; RECEPTOR CAPPING;
D O I
10.1172/JCI115027
中图分类号
R-3 [医学研究方法]; R3 [基础医学];
学科分类号
1001 ;
摘要
We studied the receptors on human cultured macrophages (MO-M-phi) responsibility for binding encapsulated and isogenic mutant acapsular strains of Cryptococcus neoformans, and whether such binding leads to a phagocytic event. Both strains required opsonization with complement components in normal human serum in order for binding to occur. Binding of the acapsular, but not the encapsulated, strain led to phagocytosis. MAb directed against any of the three defined complement receptors (CR) on MO-M-pha (CR1, CR3, and CR4) profoundly inhibited binding of serum-opsonized encapsulated (and to a lesser extent acapsular) organisms to MO-M-phi). Immunofluorescence studies demonstrated migration of CR to the area of the cryptococcal binding site. Trypsin and elastase inhibited binding of encapsulated and, to a lesser extent, acapsular yeasts to MO-M-phi. Binding of encapsulated C. neoformans was profoundly inhibited by incubation in the cold or by inhibitors of receptor capping and actin microfilaments. Thus, multiple CR appear to contribute to binding of serum-opsonized encapsulated C. neoformans by MO-M-phi. Binding is an energy-dependent process that requires conformational changes in actin yet does not lead to phagocytosis of the organism. In contrast, energy is not required for binding of acapsular yeasts by MO-M-phi and binding triggers phagocytosis.
引用
收藏
页码:528 / 535
页数:8
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