Gil M L, Villamón E, Monteagudo C, Gozalbo D, Martínez J P
Departamento de Microbiología y Ecologia, Facultad de Farmacia, Universitat de València, Spain.
FEMS Immunol Med Microbiol. 1999 Mar;23(3):229-34. doi: 10.1111/j.1574-695X.1999.tb01243.x.
We have previously described the presence of an enzymatically active form of glyceraldehyde 3-phosphate-dehydrogenase (GAPDH) in the cell surface of Candida albicans ATCC 26555 which is also a fibronectin and laminin binding protein. Immunohistochemical analysis of tissue sections from patients with disseminated candidiasis with a polyclonal antiserum to GAPDH from C. albicans (PAb anti-CA-GAPDH) revealed that the enzyme is expressed at the surface of fungal cells in infected tissues. The same PAb detected the presence of GAPDH species, with a molecular mass of approximately 33 kDa, in cell wall extracts obtained from clinical isolates of the fungus. These cell surface-bound GAPDH moieties exhibited a dose-dependent dehydrogenase activity. These results indicate that this cell surface-bound GAPDH plays a role during infection probably contributing to the attachment of fungal cells to host tissues.
我们之前曾描述过，白色念珠菌ATCC 26555的细胞表面存在一种具有酶活性形式的甘油醛-3-磷酸脱氢酶（GAPDH），它也是一种纤连蛋白和层粘连蛋白结合蛋白。用针对白色念珠菌GAPDH的多克隆抗血清（PAb抗-CA-GAPDH）对播散性念珠菌病患者的组织切片进行免疫组织化学分析，结果显示该酶在感染组织中的真菌细胞表面表达。同样的PAb在从该真菌临床分离株获得的细胞壁提取物中检测到了分子量约为33 kDa的GAPDH种类。这些细胞表面结合的GAPDH部分表现出剂量依赖性的脱氢酶活性。这些结果表明，这种细胞表面结合的GAPDH在感染过程中发挥作用，可能有助于真菌细胞附着于宿主组织。
