Almeida S R, Unterkircher C S, Camargo Z P
Department of Microbiology, Immunology and Parasitology, Federal University of São Paulo (UNIFESP), SP, Brazil.
Med Mycol. 1998 Dec;36(6):405-11. doi: 10.1080/02681219880000641.
The yeast form of Paracoccidioides brasiliensis, the causative agent of a deep mycosis in humans, is known to be phagocytized by, and to multiply inside, macrophages. In this work we describe the involvement of gp43, a major antigenic protein of P. brasiliensis, in the initial steps of attachment of the fungus to macrophages. Anti-gp43 F(ab) polyclonal fragments were capable of inhibiting phagocytosis in a concentration-dependent manner. Sheep red blood cells sensitized with purified gp43 were more endocytized than SRBC alone, and this process was also inhibited by anti-gp43 F(ab) fragments. Inhibition tests indicated the involvement of fucose and mannose residues in the phagocytosis of the fungus and of SRBC-gp43 by macrophages. Taken together, these results suggest that gp43 may be involved in the adherence and uptake of the fungus by murine peritoneal macrophages, and that this binding may be dependent on monosaccharide residues that are part of the gp43 glycoprotein.
巴西副球孢子菌是人类深部真菌病的病原体，已知其酵母形式可被巨噬细胞吞噬并在巨噬细胞内繁殖。在本研究中，我们描述了巴西副球孢子菌的主要抗原蛋白gp43在真菌与巨噬细胞附着的初始步骤中的作用。抗gp43 F(ab)多克隆片段能够以浓度依赖的方式抑制吞噬作用。用纯化的gp43致敏的绵羊红细胞比单独的绵羊红细胞更易被内吞，并且该过程也被抗gp43 F(ab)片段抑制。抑制试验表明，岩藻糖和甘露糖残基参与了巨噬细胞对真菌和SRBC-gp43的吞噬作用。综上所述，这些结果表明gp43可能参与了小鼠腹腔巨噬细胞对真菌的黏附和摄取，并且这种结合可能依赖于作为gp43糖蛋白一部分的单糖残基。
