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1型人类免疫缺陷病毒衣壳蛋白的功能结构域

Functional domains of the capsid protein of human immunodeficiency virus type 1.

作者信息

Dorfman T, Bukovsky A, Ohagen A, Höglund S, Göttlinger H G

机构信息

Division of Human Retrovirology, Dana-Farber Cancer Institute, Boston, Massachusetts 02115.

出版信息

J Virol. 1994 Dec;68(12):8180-7. doi: 10.1128/JVI.68.12.8180-8187.1994.

DOI:10.1128/JVI.68.12.8180-8187.1994
PMID:7966609
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC237283/
Abstract

A series of deletions was introduced into the CA domain of the human immunodeficiency virus type 1 Gag polyprotein to examine its role in virus particle and core formation. The mutations resulted in two phenotypes, indicating the existence of two functionally distinct regions within the CA domain. Deletions within a conserved stretch of 20 amino acids referred to as the major homology region (MHR) and deletions C terminal to this region blocked virus replication and significantly reduced the ability to form viral particles. Deletions N terminal to the MHR also prevented virus replication, but the mutants retained the ability to assemble and release viral particles with the same efficiency as the wild-type virus. The mutant particles contained circular rather than cone-shaped cores, and while they were of a density similar to that of wild-type particles, they were more heterogeneous in size. These results indicate that CA domain sequences N terminal to the MHR are essential for the morphogenesis of the mature cone-shaped core.

摘要

在人类免疫缺陷病毒1型Gag多聚蛋白的CA结构域引入一系列缺失,以研究其在病毒颗粒和核心形成中的作用。这些突变产生了两种表型,表明CA结构域内存在两个功能不同的区域。在一段被称为主要同源区域(MHR)的20个氨基酸的保守序列内的缺失以及该区域C末端的缺失阻断了病毒复制,并显著降低了形成病毒颗粒的能力。MHR N末端的缺失也阻止了病毒复制,但突变体保留了与野生型病毒相同效率组装和释放病毒颗粒的能力。突变体颗粒含有圆形而非锥形核心,虽然它们的密度与野生型颗粒相似,但大小更不均一。这些结果表明,MHR N末端的CA结构域序列对于成熟锥形核心的形态发生至关重要。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6fb5/237283/e000329b9c0d/jvirol00021-0531-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6fb5/237283/27ee1e85658b/jvirol00021-0528-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6fb5/237283/b74b7614bcc7/jvirol00021-0528-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6fb5/237283/c3c103247798/jvirol00021-0529-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6fb5/237283/8f30cf53931f/jvirol00021-0529-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6fb5/237283/38455b35bc7c/jvirol00021-0530-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6fb5/237283/e000329b9c0d/jvirol00021-0531-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6fb5/237283/27ee1e85658b/jvirol00021-0528-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6fb5/237283/b74b7614bcc7/jvirol00021-0528-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6fb5/237283/c3c103247798/jvirol00021-0529-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6fb5/237283/8f30cf53931f/jvirol00021-0529-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6fb5/237283/38455b35bc7c/jvirol00021-0530-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6fb5/237283/e000329b9c0d/jvirol00021-0531-a.jpg

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