Use of alternative receptors different than α-dystroglycan by selected isolates of lymphocytic choriomeningitis virus
Use of alternative receptors different than α-dystroglycan by selected isolates of lymphocytic choriomeningitis virus
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DOI：
10.1016/j.virol.2004.05.009
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发表时间：
2004-08-01
期刊：
影响因子：
3.7
通讯作者：
Oldstone, MBA
中科院分区：
文献类型：
--
作者：
Kunz, S;Sevilla, N;Oldstone, MBA
病毒的长期感染允许产生变异，这些变异在某些组织中进化出特定的生长优势，并可能显示出改变的疾病潜力。这些变异体的选择受宿主组织的影响，通常涉及病毒与受体的相互作用。在这里，我们报告了几个表现不同疾病模式的淋巴细胞性脉络膜脑膜炎病毒(LCMV)分离株对受体使用的研究。与我们之前的研究一致，我们发现，除了一个例外，多个LCMV变体导致免疫反应抑制，与其细胞受体α-DG(α-DG)高亲和力结合，并依赖α-DG进入和感染。例外情况也与α-DG强烈结合，但不依赖于α-DG进入和感染。相反，那些不抑制免疫反应的LCMV变体要么对α-DG表现出低的结合亲和力，要么没有结合，并使用替代受体作为α-DG的补充或替代来进入和感染。对于所有的α-DG结合变异体，α-DG是表达DG的细胞的首选受体，因为可溶性α-DG阻止了DG缺陷细胞的感染，表明α-DG与病毒表面的病毒糖蛋白(GP)的结合干扰了GP与替代受体的相互作用。对LCMV的选择性受体(S)的生化鉴定表明，它们要么是蛋白质(S)，要么是蛋白质结合的实体。(C)2004 Elsevier Inc.保留所有权利。
Long-term infections with viruses permit the generation of variants that evolve specific growth advantages in certain tissues and may show altered disease potentials. The selection of such variants is influenced by the host tissue and often involves virus-receptor interactions. Here we report studies of receptor usage by several lymphocytic choriomeningitis virus (LCMV) isolates that expressed different disease patterns. Consistent with our previous studies, we found that, with one exception, multiple LCMV variants that cause suppression of immune responses bound with high affinity to their cellular receptor alpha-dystroglycan (alpha-DG) and were dependent on alpha-DG for entry and infection. The exception also bound strongly to alpha-DG but was not dependent on alpha-DG for entry and infection. In contrast, those variants of LCMV that do not suppress the immune response either displayed low or no binding affinity for alpha-DG and used alternative receptors in addition to or instead of alpha-DG for entry and infection. For all alpha-DG binding variants, alpha-DG represents the preferred receptor in DG-expressing cells, as soluble alpha-DG blocked their infection of DG-deficient cells, indicating that binding of alpha-DG to the viral glycoprotein (GP) at the virion surface interferes with the GP's interaction with the alternative receptor. Biochemical characterization of the alternative receptor(s) for LCMV indicated that they are either protein(s) or protein-bound entities. (C) 2004 Elsevier Inc. All rights reserved.