与福氏耐格里阿米巴表面膜相关的一种热稳定细胞溶解蛋白的激活。
Activation of a heat-stable cytolytic protein associated with the surface membrane of Naegleria fowleri.
作者信息
Lowrey D M, McLaughlin J
出版信息
Infect Immun. 1985 Nov;50(2):478-82. doi: 10.1128/iai.50.2.478-482.1985.
Abstract
Surface membrane-enriched fractions of Naegleria fowleri obtained after isopycnic centrifugation experiments contain a potent cytolytic activity as determined by hemolysis and 51Cr release assays. This surface membrane cytolysin was unaffected by a treatment at 75 degrees C for 30 min and accounted for 70 to 90% of cytolysis by whole-cell lysates of amoebae. This heat resistance as well as intimate membrane association distinguished the surface membrane cytolytic activity from a second heat-labile cytolytic activity which appears to be latent within lysosomes. The surface membrane cytolysin was found to be specifically activated by diluted samples of lysosomal fractions. The possible role of this surface membrane cytotoxin in the pathogenicity of N. fowleri is discussed.
摘要
通过等密度离心实验获得的福氏耐格里阿米巴表面膜富集组分，经溶血和⁵¹Cr释放试验测定，具有强大的细胞溶解活性。这种表面膜溶细胞素在75℃处理30分钟后不受影响，并且占变形虫全细胞裂解物细胞溶解的70%至90%。这种耐热性以及与膜的紧密结合，使表面膜细胞溶解活性与第二种对热不稳定的细胞溶解活性区分开来，后者似乎潜伏在溶酶体内。发现表面膜溶细胞素可被溶酶体组分的稀释样品特异性激活。讨论了这种表面膜细胞毒素在福氏耐格里阿米巴致病性中的可能作用。
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