+検索条件
-Structure paper
タイトル | In vitro protease cleavage and computer simulations reveal the HIV-1 capsid maturation pathway. |
---|---|
ジャーナル・号・ページ | Nat Commun, Vol. 7, Page 13689, Year 2016 |
掲載日 | 2016年12月13日 |
著者 | Jiying Ning / Gonca Erdemci-Tandogan / Ernest L Yufenyuy / Jef Wagner / Benjamin A Himes / Gongpu Zhao / Christopher Aiken / Roya Zandi / Peijun Zhang / |
PubMed 要旨 | HIV-1 virions assemble as immature particles containing Gag polyproteins that are processed by the viral protease into individual components, resulting in the formation of mature infectious particles. ...HIV-1 virions assemble as immature particles containing Gag polyproteins that are processed by the viral protease into individual components, resulting in the formation of mature infectious particles. There are two competing models for the process of forming the mature HIV-1 core: the disassembly and de novo reassembly model and the non-diffusional displacive model. To study the maturation pathway, we simulate HIV-1 maturation in vitro by digesting immature particles and assembled virus-like particles with recombinant HIV-1 protease and monitor the process with biochemical assays and cryoEM structural analysis in parallel. Processing of Gag in vitro is accurate and efficient and results in both soluble capsid protein and conical or tubular capsid assemblies, seemingly converted from immature Gag particles. Computer simulations further reveal probable assembly pathways of HIV-1 capsid formation. Combining the experimental data and computer simulations, our results suggest a sequential combination of both displacive and disassembly/reassembly processes for HIV-1 maturation. |
リンク | Nat Commun / PubMed:27958264 / PubMed Central |
手法 | EM (サブトモグラム平均) / EM (らせん対称) |
解像度 | 18.0 - 22.0 Å |
構造データ | EMDB-8403: EMDB-8404: |
由来 |
|