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1型人类免疫缺陷病毒基质蛋白N端区域的突变会阻断Gag前体的细胞内运输。

Mutations in the N-terminal region of human immunodeficiency virus type 1 matrix protein block intracellular transport of the Gag precursor.

作者信息

Yuan X, Yu X, Lee T H, Essex M

机构信息

Department of Cancer Biology, Harvard School of Public Health, Boston, Massachusetts 02115.

出版信息

J Virol. 1993 Nov;67(11):6387-94. doi: 10.1128/JVI.67.11.6387-6394.1993.

DOI:10.1128/JVI.67.11.6387-6394.1993
PMID:8411340
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC238073/
Abstract

The matrix domain of human immunodeficiency virus type 1 Gag polyprotein was studied for its role in virus assembly. Deletion and substitution mutations caused a dramatic reduction in virus production. Mutant Gag polyproteins were myristoylated and had a high affinity for membrane association. Immunofluorescence staining revealed a large accumulation of mutant Gag precursors in the cytoplasm, while wild-type Gag proteins were primarily associated with the cell surface membrane. These results suggest a defect in intracellular transport of the mutant Gag precursors. Thus, in addition to myristoylation, the N-terminal region of the matrix domain is involved in determining Gag protein transport to the plasma membrane. Wild-type Gag polyproteins interacted with and efficiently packaged mutant Gag into virions. This finding is consistent with the hypothesis that intermolecular interaction of Gag polyproteins might occur in the cytoplasm prior to being transported to the assembly site on the plasma membrane.

摘要

对1型人类免疫缺陷病毒Gag多聚蛋白的基质结构域在病毒组装中的作用进行了研究。缺失和替换突变导致病毒产生显著减少。突变的Gag多聚蛋白被肉豆蔻酰化，并且对膜结合具有高亲和力。免疫荧光染色显示突变的Gag前体在细胞质中大量积累，而野生型Gag蛋白主要与细胞表面膜相关。这些结果表明突变的Gag前体在细胞内运输存在缺陷。因此，除了肉豆蔻酰化之外，基质结构域的N端区域还参与决定Gag蛋白向质膜的运输。野生型Gag多聚蛋白与突变的Gag相互作用并有效地将其包装到病毒粒子中。这一发现与以下假设一致，即Gag多聚蛋白的分子间相互作用可能在被运输到质膜上的组装位点之前在细胞质中发生。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1dde/238073/fd4d4da7bfdf/jvirol00032-0070-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1dde/238073/fe022eb1c3d0/jvirol00032-0067-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1dde/238073/52707c337d3f/jvirol00032-0067-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1dde/238073/b9a4fac52931/jvirol00032-0068-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1dde/238073/e880628d230f/jvirol00032-0069-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1dde/238073/8472ed10013e/jvirol00032-0070-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1dde/238073/fd4d4da7bfdf/jvirol00032-0070-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1dde/238073/fe022eb1c3d0/jvirol00032-0067-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1dde/238073/52707c337d3f/jvirol00032-0067-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1dde/238073/b9a4fac52931/jvirol00032-0068-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1dde/238073/e880628d230f/jvirol00032-0069-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1dde/238073/8472ed10013e/jvirol00032-0070-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1dde/238073/fd4d4da7bfdf/jvirol00032-0070-b.jpg

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