Human immunodeficiency virus type 1 matrix protein assembles on membranes as a hexamer
Human immunodeficiency virus type 1 matrix protein assembles on membranes as a hexamer
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DOI：
10.1128/jvi.02122-06
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发表时间：
2007-02-01
影响因子：
5.4
通讯作者：
Barklis, Eric
中科院分区：
文献类型：
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作者：
Alfadhli, Ayna;Huseby, Doug;Barklis, Eric
人类免疫缺陷病毒1型（HIV-1）结构前体Gag（PrGag）蛋白的膜结合基质（MA）结构域在溶液中寡聚为三聚体，并在三维中结晶为三聚体单元。已经提出了许多模型来解释MA三聚体如何与PrGag衣壳（CA）N-末端结构域（NTD）对齐，其组装六方晶格。我们研究了自然豆蔻酰化的HIV-1基质（MyrMA）和基质加衣壳（MyrMACA）蛋白在体外膜上的结合。出乎意料的是，MyrMA和MyrMACA蛋白都组装六角笼状晶格的磷脂酰丝氨酸胆固醇膜。膜结合的MyrMA蛋白没有组织成三聚体单位，而是组织成六聚体环。我们的研究结果产生了一个模型，其中MA结构域直接堆叠在未成熟颗粒中的NTD六聚体上方，并且它们对HIV组装和MA与病毒膜糖蛋白之间的相互作用具有影响。
The membrane-binding matrix (MA) domain of the human immunodeficiency virus type 1 (HIV-1) structural precursor Gag (PrGag) protein oligomerizes in solution as a trimer and crystallizes in three dimensions as a trimer unit. A number of models have been proposed to explain how MA trimers; might align with respect to PrGag capsid (CA) N-terminal domains (NTDs), which assemble hexagonal lattices. We have examined the binding of naturally myristoylated HIV-1 matrix (MyrMA) and matrix plus capsid (MyrMACA) proteins on membranes in vitro. Unexpectedly, MyrMA and MyrMACA proteins both assembled hexagonal cage lattices on phosphatidylserine-cholesterol membranes. Membrane-bound MyrMA proteins did not organize into trimer units but, rather, organized into hexamer rings. Our results yield a model in which MA domains stack directly above NTD hexamers in immature particles, and they have implications for HIV assembly and interactions between MA and the viral membrane glycoproteins.