R肽切割增强莫洛尼鼠白血病病毒Env中亚基间二硫键的融合控制异构化。
R-Peptide cleavage potentiates fusion-controlling isomerization of the intersubunit disulfide in Moloney murine leukemia virus Env.
作者信息
Löving Robin, Li Kejun, Wallin Michael, Sjöberg Mathilda, Garoff Henrik
机构信息
Department of Biosciences and Nutrition, Karolinska Institute, S-141 57 Huddinge, Sweden.
出版信息
J Virol. 2008 Mar;82(5):2594-7. doi: 10.1128/JVI.02039-07. Epub 2007 Dec 19.
Abstract
Fusion of the membrane of the Moloney murine leukemia virus (Mo-MLV) Env protein is facilitated by cleavage of the R peptide from the cytoplasmic tail of its TM subunit, but the mechanism for this effect has remained obscure. The fusion is also controlled by the isomerization of the intersubunit disulfide of the Env SU-TM complex. In the present study, we used several R-peptide-cleavage-inhibited virus mutants to show that the R peptide suppresses the isomerization reaction in both in vitro and in vivo assays. Thus, the R peptide affects early steps in the activation pathway of murine leukemia virus Env.
摘要
莫洛尼鼠白血病病毒（Mo-MLV）Env蛋白的膜融合通过其跨膜（TM）亚基胞质尾的R肽裂解得以促进，但其作用机制仍不清楚。Env的表面亚基（SU）-跨膜亚基（TM）复合物的亚基间二硫键异构化也控制着融合。在本研究中，我们使用了几种R肽裂解抑制的病毒突变体，以表明R肽在体外和体内试验中均抑制异构化反应。因此，R肽影响鼠白血病病毒Env激活途径的早期步骤。
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本文引用的文献
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Receptor-triggered but alkylation-arrested env of murine leukemia virus reveals the transmembrane subunit in a prehairpin conformation.受体触发但被烷基化阻断的鼠白血病病毒包膜蛋白揭示了处于前发夹构象的跨膜亚基。
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Cytoplasmic tail of Moloney murine leukemia virus envelope protein influences the conformation of the extracellular domain: implications for mechanism of action of the R Peptide.莫洛尼鼠白血病病毒包膜蛋白的细胞质尾部影响细胞外结构域的构象：对R肽作用机制的启示。
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