Identification of a concanavalin A-binding antigen of the cell surface of Sporothrix schenckii.

O C Lima, L M Bezerra
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引用次数: 29

Abstract

Sporothrix schenckii (1099-18) cell wall peptido-rhamnomannan (CWPR) was fractionated by affinity chromatography with Concanavalin A. The Con A-bound and Con A-unbound fractions were probed with an anti-S. schenckii rabbit serum. We identified within the Con A-bound fraction three main antigens with approximate molecular weights of 84, 70 and 58 kDa. Glycopeptide beta-elimination reduced rabbit antiserum reactivity for the 84 kDa antigen (gp84) with concomittant enhanced reactivity for the 70 kDa antigen (gp70). By Western blot with Con A-HRP conjugate we demonstrated that gp84 strongly reacted with this lectin and this was the predominant antigen identified. The gp84 antigen was also demonstrated to be present on other S. schenckii strains.

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申氏孢子丝菌细胞表面豆蛋白a结合抗原的鉴定。
用Concanavalin a亲和层析法分离申克孢子菌(1099-18)细胞壁肽-鼠李甘露聚糖(CWPR),用抗s检测Con a结合和Con a未结合部分。申氏兔血清。我们在Con a结合片段中鉴定出三种主要抗原,分子量分别为84、70和58 kDa。糖肽β消除降低了兔对84 kDa抗原(gp84)的抗血清反应性,同时增强了对70 kDa抗原(gp70)的反应性。通过Western blot与Con A-HRP偶联,我们证实gp84与该凝集素强烈反应,这是鉴定的优势抗原。gp84抗原也被证实存在于其他申克沙门氏菌株上。
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