Candida glabrata (C. glabrata) cell wall proteins play a role in virulence and in initial host immune recognition and responses. We isolated and characterized C. glabrata cell wall proteases from a clinical hospital C. glabrata T-1638 blood isolate and estimated the enzymatic activities and their ability to degrade gelatin and processing proMMP-8 and assess the regulation of these proteases with salt treatment, mercaptoethanol and fermented lingonberry juice from Vaccinium vitis idaea L. The cell wall proteases were enzymatically released from the cell wall and beta- 1,3- bonded proteases were fractioned into 10–50 kDa and >50 kDa fractions with anionic DEAE-sepharose ion-exchange chromatography and gel filtration. Proteins were monitored and analyzed with MDPF- zymography, and five gelatinolytic bands were cut out from a parallel silver-stained gel for the LC- MS/MS analysis. The proteases lacked a signal sequence, indicating that they are moonlighting proteases. Human proMMP-8 activation assays were performed with both fractions and verified by western-immunoblot using aMMP-8 specific antibody. Inhibition of proMMP-8 conversion to the lower molecular active enzyme species were demonstrated with fermented lingonberry juice. The results indicate that moonlighting proteases may play a role in the virulence of C. glabrata.

光滑念珠菌（C. glabrata）细胞壁蛋白在毒力和初始宿主免疫识别和反应中发挥作用。我们从临床C. glabrata T-1638血液分离物中分离并鉴定了C. glabrata细胞壁蛋白酶，并评估了其酶活性及其降解明胶和加工proMMP-8的能力，并通过盐处理，巯基乙醇评估了这些蛋白酶的调节和越橘葡萄的发酵越橘汁L.细胞壁蛋白酶通过酶从细胞壁中释放出来，β-1,3-键合的蛋白酶通过阴离子DEAE-琼脂糖离子交换色谱和凝胶过滤分离为10-50 kDa和> 50 kDa的级分。使用MDPF酶谱仪监测和分析蛋白质，并从平行的银染凝胶上切出五​​个明胶分解带，用于LC-MS / MS分析。蛋白酶缺乏信号序列，表明它们是月光下的蛋白酶。对两个部分均进行了人类proMMP-8激活测定，并使用aMMP-8特异性抗体通过western免疫印迹进行了验证。发酵越橘汁证明了proMMP-8转化为低分子活性酶的抑制作用。结果表明，月光照蛋白酶可能在鸡的毒力中起作用。光滑念珠菌。