溶组织内阿米巴凝集素细胞质结构域对黏附及毒力的调控，该结构域含有一个β2整合素基序。
Regulation of adherence and virulence by the Entamoeba histolytica lectin cytoplasmic domain, which contains a beta2 integrin motif.
作者信息
Vines R R, Ramakrishnan G, Rogers J B, Lockhart L A, Mann B J, Petri W A
机构信息
Department of Microbiology, University of Virginia, Charlottesville, Virginia 22908, USA.
出版信息
Mol Biol Cell. 1998 Aug;9(8):2069-79. doi: 10.1091/mbc.9.8.2069.
Abstract
Killing of human cells by the parasite Entamoeba histolytica requires adherence via an amebic cell surface lectin. Lectin activity in the parasite is regulated by inside-out signaling. The lectin cytoplasmic domain has sequence identity with a region of the beta2 integrin cytoplasmic tail implicated in regulation of integrin-mediated adhesion. Intracellular expression of a fusion protein containing the cytoplasmic domain of the lectin has a dominant negative effect on extracellular lectin-mediated cell adherence. Mutation of the integrin-like sequence abrogates the dominant negative effect. Amebae expressing the dominant negative mutant are less virulent in an animal model of amebiasis. These results suggest that inside-out signaling via the lectin cytoplasmic domain may control the extracellular adhesive activity of the amebic lectin and provide in vivo demonstration of the lectin's role in virulence.
摘要
溶组织内阿米巴寄生虫杀死人类细胞需要通过一种阿米巴细胞表面凝集素进行黏附。寄生虫中的凝集素活性受外向内信号传导调节。凝集素细胞质结构域与β2整合素细胞质尾部中涉及整合素介导黏附调节的区域具有序列同源性。含有凝集素细胞质结构域的融合蛋白在细胞内表达对细胞外凝集素介导的细胞黏附具有显性负效应。整合素样序列的突变消除了显性负效应。在阿米巴病动物模型中，表达显性负突变体的阿米巴毒性较低。这些结果表明，通过凝集素细胞质结构域的外向内信号传导可能控制阿米巴凝集素的细胞外黏附活性，并在体内证明了凝集素在毒力中的作用。
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