A phagocytosis mutant of Entamoeba histolytica is less virulent due to deficient proteinase expression and release
A phagocytosis mutant of Entamoeba histolytica is less virulent due to deficient proteinase expression and release
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DOI：
10.1016/j.exppara.2006.08.004
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发表时间：
2007-02-01
影响因子：
2.1
通讯作者：
Reed, Sharon L.
中科院分区：
文献类型：
--
作者：
Hirata, Ken K.;Que, Xuchu;Reed, Sharon L.
半胱氨酸蛋白酶是溶组织内阿米巴入侵过程中释放的关键毒力因子。我们使用了溶组织内阿米巴菌株 HM-1:IMSS 的化学突变体（克隆 L6），该突变体缺乏毒力、吞噬作用和半胱氨酸蛋白酶活性，以帮助确定半胱氨酸蛋白酶释放的机制。野生型 HM-1 的所有半胱氨酸蛋白酶基因均存在于 L6 突变体基因组中，但三种主要表达的蛋白酶 ehcp1、ehcp2 和 ehcp5 在 L6 中均以较低水平转录、翻译和释放。我们假设该突变体可能缺乏吞噬作用和胞吐作用所需的中心蛋白，例如钙结合蛋白 1 EhCaBP1。我们发现 L6 中 EhCaBP1 的 mRNA 和蛋白酶水平均下降。这些发现提供了吞噬作用、多种半胱氨酸蛋白酶的被动释放和该溶组织内阿米巴突变体的毒力减弱之间的重要联系。 (c) 2006 Elsevier Inc. 保留所有权利。
Cysteine proteinases are key virulence factors of Entamoeba histolytica that are released during the process of invasion. We used a chemical mutant of E histolytica strain HM-1:IMSS, clone L6, which is deficient in virulence, phagocytosis, and cysteine proteinase activity to help define the mechanisms of cysteine proteinase release. All cysteine proteinase genes of wild type HM-1 were present in the L6 mutant genome, but three of the major expressed proteinases, ehcp1, ehcp2, and ehcp5 were both transcribed, translated, and released at lower levels in L6. We hypothesized that a central protein such as the calcium binding protein 1, EhCaBP1, which is required for both phagocytosis and exocytosis might be deficient in this mutant. We found that both mRNA and proteinase levels of EhCaBP1 were decreased in L6. These findings provide an important link between phagocytosis, passive release of multiple cysteine proteinases, and attenuated virulence of this E. histolytica mutant. (c) 2006 Elsevier Inc. All rights reserved.