A FIBRONECTIN RECEPTOR ON CANDIDA-ALBICANS MEDIATES ADHERENCE OF THE FUNGUS TO EXTRACELLULAR-MATRIX
A FIBRONECTIN RECEPTOR ON CANDIDA-ALBICANS MEDIATES ADHERENCE OF THE FUNGUS TO EXTRACELLULAR-MATRIX
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DOI：
10.1093/infdis/163.3.604
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发表时间：
1991-03-01
影响因子：
6.4
通讯作者：
SMITH, RL
中科院分区：
文献类型：
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作者：
KLOTZ, SA;SMITH, RL
测定了细胞外基质(ECM)蛋白纤维连接蛋白与白色念珠菌的结合，并研究了该真菌对固定化ECM蛋白、纤维连接蛋白、层粘连蛋白、I型和IV型胶原以及内皮下ECM的粘附性。未标记的人血浆纤维连接蛋白和Arg-Gly-Asp(RGD)、Gly-Arg-Gly-Gly-Glu-Ser-Pro(GRGESP)和Gly-Arg-Gly-Gly-Asp-Thr-Pro(GRGDTP)可抑制I-125标记的纤维连接蛋白与真菌的结合，但Gly-Arg-Gly-Asp-Ser-Pro不抑制结合。可溶性纤维连接蛋白、RGD、GRGESP和GRGDTP也以一种复杂的方式抑制真菌与单个固定化ECM蛋白的黏附，但只有可溶性纤维连接蛋白(10(-7)M)抑制真菌与内皮下ECM的黏附。因此，白念珠菌至少拥有一种细胞表面受体，可以与可被多肽抑制的可溶性纤维连接蛋白结合。这种受体显然用于将真菌与固定化的ECM蛋白和内皮下ECM结合，并可能通过提供微生物与ECM蛋白的黏附而在血液真菌引发播散性疾病中发挥作用。
Binding of fibronectin, an extracellular matrix (ECM) protein, to Candida albicans was measured, and adherence of the fungus to immobilized ECM proteins, fibronectin, laminin, types I and IV collagen, and subendothelial ECM was studied. I-125-labeled fibronectin was inhibited from binding to the fungus by unlabeled human plasma fibronectin and by Arg-Gly-Asp (RGD), Gly-Arg-Gly-Glu-Ser-Pro (GRGESP), and Gly-Arg-Gly-Asp-Thr-Pro (GRGDTP), but binding was not inhibited by Gly-Arg-Gly-Asp-Ser-Pro. Soluble fibronectin, RGD, GRGESP, and GRGDTP also inhibited fungal adherence to the individual immobilized ECM proteins in a complex pattern, but only soluble fibronectin (10(-7) M) inhibited fungal adherence to subendothelial ECM. Thus, C. albicans possesses at least one type of cell surface receptor for binding soluble fibronectin that can be inhibited with peptides. This receptor apparently is used to bind the fungus to immobilized ECM proteins and to subendothelial ECM and may play a role in the initiation of disseminated disease by bloodborne fungi by providing for adherence of the microorganisms to ECM proteins.