热诱导型白色念珠菌atp结合蛋白可被感染患者血清识别。

R Swoboda, S Miyasaki, D Greenspan, J S Greenspan
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引用次数: 21

摘要

用ATP亲和层析法从白色念珠菌提取物中分离出4个蛋白。这些蛋白在25℃至37℃的细胞提取物中含量较高,但在25℃的细胞中含量较低。这些蛋白的分子质量(38-42 kDa, 66-68 kDa, 70-72 kDa和74-76 kDa)与已发表的白色念珠菌热休克蛋白的大小一致。口腔和/或食管白色念珠菌感染患者的血清可识别这四种蛋白中的三种,在所有测试病例中均有70-72 kDa蛋白反应。抗体与其他两种蛋白(38-42 kDa和74-76 kDa)的结合情况因患者而异。IgA抗体是这些粘膜白色念珠菌感染的主要免疫球蛋白类。IgA抗体滴度可能具有诊断价值,似乎与感染的严重程度相关,与口腔感染相比,食道感染的IgA抗体滴度更高。与这些蛋白结合的抗体是特异性的,因为血清没有显示出与细菌或HeLa细胞热休克蛋白相同的增强识别。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Heat-inducible ATP-binding proteins of Candida albicans are recognized by sera of infected patients.

Four proteins from Candida albicans extracts have been isolated by ATP affinity chromatography. These proteins were found to be at elevated levels in extracts of cells raised from 25 degrees C to 37 degrees C, but were present at low levels in cells grown at 25 degrees C. The molecular masses of the proteins (38-42 kDa, 66-68 kDa, 70-72 kDa and 74-76 kDa) correspond to the published sizes of C. albicans heat-shock proteins. Three of the four proteins were recognized by the sera of patients with oral and/or oesophageal C. albicans infections, with the 70-72 kDa protein reacting in all cases tested. Binding of antibodies to two of the other proteins (38-42 kDa and 74-76 kDa) differed from patient to patient. IgA antibodies were the dominant immunoglobulin class in these mucosal C. albicans infections. The IgA antibody titre may be of diagnostic value and seemed to be correlated to the severity of infections, with a higher level in oesophageal infections compared to oral infections. Antibody binding to these proteins was specific as the sera did not show the same enhanced recognition with bacterial or HeLa cell heat-shock proteins.

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