Interaction of HIV-1 gp41 core with NPF motif in Epsin - Implication in endocytosis of HIV
Interaction of HIV-1 gp41 core with NPF motif in Epsin - Implication in endocytosis of HIV
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HIV-1 gp41 核心与 Epsin 中 NPF 基序的相互作用 - 对 HIV 内吞作用的影响
DOI：
10.1074/jbc.m800525200
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发表时间：
2008-05-30
影响因子：
4.8
通讯作者：
Chen, Ying-Hua
中科院分区：
文献类型：
--
作者：
Huang, Jing-He;Qi, Zhi;Chen, Ying-Hua
人类免疫缺陷病毒1型（HIV-1）gp 41核心在病毒和靶细胞膜之间的融合中起重要作用。我们先前鉴定了HIV-1 gp 41核心结合基序HXXNPF（其中X是任何氨基酸残基）。在这项研究中，我们发现Asn，Pro和Phe是gp 41核心结合的关键残基。在Epsin-I（470 - 499）中存在两个NPF基序，Epsin-I是Epsin的片段，其是内吞作用的必需辅助因子，其可以通过与脂质相互作用而停靠到质膜。Epsin-1-（470-499）与多肽N36（L 8）C34形成的gp 41核心结构结合，并与含有核心结构的重组可溶性gp 41相互作用。含有Epsin-1-（470 - 499）序列的合成肽可以有效地阻断HIV- 1病毒粒子通过内吞途径进入SupT 1 T细胞。这些结果表明，Epsin和gp 41核心之间的相互作用，这可能是目前在靶细胞膜，可能是必要的内吞作用的HIV-1，HIV-1进入靶细胞的替代途径。
The human immunodeficiency virus, type 1 (HIV-1), gp41 core plays an important role in fusion between viral and target cell membranes. We previously identified an HIV-1 gp41 core-binding motif HXXNPF (where X is any amino acid residue). In this study, we found that Asn, Pro, and Phe were the key residues for gp41 core binding. There are two NPF motifs in Epsin-l(470 - 499), a fragment of Epsin, which is an essential accessory factor of endocytosis that can dock to the plasma membrane by interacting with the lipid. Epsin-1-(470-499) bound significantly to the gp41 core formed by the polypeptide N36(L8)C34 and interacted with the recombinant soluble gp41 containing the core structure. A synthetic peptide containing the Epsin-1-(470 - 499) sequence could effectively block entry of HIV- 1 virions into SupT1 T cells via the endocytosis pathway. These results suggest that interaction between Epsin and the gp41 core, which may be present in the target cell membrane, is probably essential for endocytosis of HIV-1, an alternative pathway of HIV-1 entry into the target cell.