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全长猫免疫缺陷病毒衣壳蛋白的晶体结构显示在没有 N 端脯氨酸的情况下存在 N 端 β-发夹。

Crystal Structure of the Full-Length Feline Immunodeficiency Virus Capsid Protein Shows an N-Terminal β-Hairpin in the Absence of N-Terminal Proline.

机构信息

Equipe Rétrovirus et Biochimie Structurale, Université de Lyon, CNRS, MMSB, UMR 5086 CNRS/Université de Lyon, IBCP, Lyon 69367 CEDEX 07, France.

Laboratorio de Moléculas Bioactivas, Centro Universitario Regional Litoral Norte, Universidad de la República, Paysandú 60000, Uruguay.

出版信息

Viruses. 2017 Nov 9;9(11):335. doi: 10.3390/v9110335.

DOI:10.3390/v9110335
PMID:29120364
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5707542/
Abstract

Feline immunodeficiency virus (FIV) is a member of the Retroviridae family. It is the causative agent of an acquired immunodeficiency syndrome (AIDS) in cats and wild felines. Its capsid protein (CA) drives the assembly of the viral particle, which is a critical step in the viral replication cycle. Here, the first atomic structure of full-length FIV CA to 1.67 Å resolution is determined. The crystallized protein exhibits an original tetrameric assembly, composed of dimers which are stabilized by an intermolecular disulfide bridge induced by the crystallogenesis conditions. The FIV CA displays a standard α-helical CA topology with two domains, separated by a linker shorter than other retroviral CAs. The β-hairpin motif at its amino terminal end, which interacts with nucleotides in HIV-1, is unusually long in FIV CA. Interestingly, this functional β-motif is formed in this construct in the absence of the conserved N-terminal proline. The FIV CA exhibits a Arg-Pro bond in the CypA-binding loop, which is absent in known structures of lentiviral CAs. This structure represents the first tri-dimensional structure of a functional, full-length FIV CA.

摘要

猫免疫缺陷病毒（FIV）是逆转录病毒科的一员。它是导致猫和野生猫科动物获得性免疫缺陷综合征（AIDS）的病原体。它的衣壳蛋白（CA）驱动病毒颗粒的组装，这是病毒复制周期中的关键步骤。在这里，以 1.67Å 的分辨率确定了全长 FIV CA 的第一个原子结构。结晶蛋白表现出原始的四聚体组装，由二聚体组成，这些二聚体通过晶体形成条件诱导的分子间二硫键稳定。FIV CA 显示出标准的α-螺旋 CA 拓扑结构，由两个结构域组成，通过比其他逆转录病毒 CA 更短的接头分开。其氨基末端的β发夹模体与 HIV-1 中的核苷酸相互作用，在 FIV CA 中异常长。有趣的是，在这个结构中，这个功能β模体是在没有保守的 N 端脯氨酸的情况下形成的。FIV CA 在 CypA 结合环中显示出 Arg-Pro 键，而在已知的慢病毒 CA 结构中不存在。该结构代表了第一个功能性全长 FIV CA 的三维结构。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f795/5707542/12b5385e816d/viruses-09-00335-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f795/5707542/af55f50ab79e/viruses-09-00335-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f795/5707542/5c658b41bae8/viruses-09-00335-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f795/5707542/4f06b4a153b1/viruses-09-00335-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f795/5707542/99f2f25b7ed6/viruses-09-00335-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f795/5707542/12b5385e816d/viruses-09-00335-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f795/5707542/af55f50ab79e/viruses-09-00335-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f795/5707542/5c658b41bae8/viruses-09-00335-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f795/5707542/4f06b4a153b1/viruses-09-00335-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f795/5707542/99f2f25b7ed6/viruses-09-00335-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f795/5707542/12b5385e816d/viruses-09-00335-g005.jpg

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