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HIV-1包膜蛋白V3环中的N-聚糖对CXCR-4依赖的融合而非CCR-5依赖的融合的重要性。

Importance of the N-glycan in the V3 loop of HIV-1 envelope protein for CXCR-4- but not CCR-5-dependent fusion.

作者信息

Nakayama E E, Shioda T, Tatsumi M, Xin X, Yu D, Ohgimoto S, Kato A, Sakai Y, Ohnishi Y, Nagai Y

机构信息

Department of Viral Infection, Institute of Medical Science, University of Tokyo, Japan.

出版信息

FEBS Lett. 1998 Apr 24;426(3):367-72. doi: 10.1016/s0014-5793(98)00375-5.

Abstract

The V3 region of HIV-1 envelope protein possesses a single N-linked sugar chain, which is conserved in most HIV-1 strains. We studied its role in the life cycle of HIV-1 strains with different co-receptor usage. Removal of the glycan appeared to cause a marked reduction of CXCR-4- but not CCR-5-dependent virus entry. A basic amino acid substitution at the 11th position of V3 markedly compensated for the removal of the N-glycan. These results indicate that the N-glycan plays an important role for CXCR-4-dependent virus entry and that this role is exerted in a particular context of the peptide backbone.

摘要

HIV-1包膜蛋白的V3区域有一条单一的N-连接糖链,在大多数HIV-1毒株中是保守的。我们研究了其在具有不同共受体使用情况的HIV-1毒株生命周期中的作用。去除聚糖似乎会导致依赖CXCR-4而非CCR-5的病毒进入显著减少。V3第11位的碱性氨基酸取代显著补偿了N-聚糖的去除。这些结果表明,N-聚糖对依赖CXCR-4的病毒进入起重要作用,且该作用在肽骨架的特定背景下发挥。

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