Specific binding of recombinant foamy virus envelope protein to host cells correlates with susceptibility to infection

Specific binding of recombinant foamy virus envelope protein to host cells correlates with susceptibility to infection
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DOI:
10.1006/viro.1998.9570
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发表时间:
1999-03-15
期刊:
影响因子:
3.7
通讯作者:
Schneider, J
Schneider, J
中科院分区:
医学3区
文献类型:
--
作者:
Herchenröder, O;Moosmayer, D;Schneider, J

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被引文献

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使用两种类型的重组包膜蛋白 (Env) 研究了猿猴泡沫病毒 (FV) 与其假定细胞受体的相互作用。 BHK-21 细胞中 fun 长度 Env 的瞬时表达诱导合胞体形成。然而,选定的稳定转染子与初始细胞融合,但彼此不融合。 Env 表面结构域与人 IgG1 重链 Fe 片段 (EnvSU-Ig) 的可溶性融合蛋白在杆状病毒表达系统中产生,纯化至均质,并用于结合和竞争分析。 EnvSU-Ig 但不相关的 lg 融合蛋白特异性地与细胞结合。中和血清阻断了EnvSU-Ig的结合,反之亦然,血清介导的中和被嵌合蛋白消除。在表达 Env 的靶细胞中观察到 EnvSU-Ig 结合和 Ri 敏感性同时降低。尽管 EnvSU-Ig 不能抑制 FV 感染,很可能是由于多价病毒-细胞相互作用导致其置换,但这种二价配体应该有助于表征功能并识别普遍存在的 FV 受体。 (C) 1999 年学术出版社。
The interaction of simian foamy viruses (FVs) with their putative cellular receptor(s) was studied with two types of recombinant envelope protein (Env). Transient expression of fun-length Env in BHK-21 cells induced syncytia formation. However, selected stable transfectants fused with naive cells but not with each other. A soluble fusion protein of the Env surface domain with the Fe fragment of a human IgG1 heavy chain (EnvSU-Ig) was produced in the baculovirus expression system, purified to homogeneity, and used for binding and competition analyses. EnvSU-Ig but not unrelated lg fusion proteins bound to cells specifically. Neutralizing serum blocked binding of EnvSU-Ig and, vice versa, serum-mediated neutralization was abrogated by the chimeric protein. Concomitant reduction of EnvSU-Ig binding and Ri susceptibility was seen in Env-expressing target cells. Although EnvSU-Ig did not inhibit FV infection, very likely due to its displacement by multivalent virus-cell interactions, this divalent ligand should help to characterize functionally and to identity the ubiquitous FV receptor. (C) 1999 Academic Press.