The multifunctional protein enolase has repeatedly been identified on the surface of numerous cell types, including a variety of pathogenic microorganisms. In Candida albicans—one of the most common fungal pathogens in humans—a surface‐exposed enolase form has been previously demonstrated to play an important role in candidal pathogenicity. In our current study, the presence of enolase at the fungal cell surface under different growth conditions was examined, and a higher abundance of enolase at the surface of C. albicans hyphal forms compared to yeast‐like cells was found. Affinity chromatography and chemical cross‐linking indicated a member of the agglutinin‐like sequence protein family—Als3—as an important potential partner required for the surface display of enolase. Analysis of Saccharomyces cerevisiae cells overexpressing Als3 with site‐specific deletions showed that the Ig‐like N‐terminal region of Als3 (aa 166–225; aa 218–285; aa 270–305; aa 277–286) and the central repeat domain (aa 434–830) are essential for the interaction of this adhesin with enolase. In addition, binding between enolase and Als3 influenced subsequent docking of host plasma proteins—high molecular mass kininogen and plasminogen—on the candidal cell surface, thus supporting the hypothesis that C. albicans can modulate plasma proteolytic cascades to affect homeostasis within the host and propagate inflammation during infection.

中文翻译：

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Als3 介导的烯醇化酶在白色念珠菌细胞表面的附着调节它们与宿主蛋白的相互作用

多功能蛋白烯醇化酶已在多种细胞类型（包括多种病原微生物）的表面被反复鉴定。在白色念珠菌（人类最常见的真菌病原体之一）中，表面暴露的烯醇酶形式先前已被证明在念珠菌致病性中起重要作用。在我们目前的研究中，检测了不同生长条件下真菌细胞表面烯醇化酶的存在，发现与酵母样细胞相比，白色念珠菌菌丝表面的烯醇化酶丰度更高。亲和层析和化学交联表明凝集素样序列蛋白家族的一个成员——Als3——是烯醇酶表面展示所需的重要潜在伙伴。分析过表达具有位点特异性缺失的 Als3 的酿酒酵母细胞表明，Als3 的 Ig 样 N 端区域（aa 166-225；aa 218-285；aa 270-305；aa 277-286）和中央重复结构域（aa 434-830）对于这种粘附素与烯醇酶的相互作用是必不可少的。此外，烯醇化酶和 Als3 之间的结合影响了宿主血浆蛋白（高分子量激肽原和纤溶酶原）在念珠菌细胞表面的后续对接，从而支持了白色念珠菌可以调节血浆蛋白水解级联反应以影响宿主内稳态并传播的假设感染期间的炎症。