Morphology and ultrastructure of retrovirus particles.

IF 1.1 Q4 BIOPHYSICS
AIMS Biophysics Pub Date : 2015-01-01 Epub Date: 2015-08-18 DOI:10.3934/biophy.2015.3.343
Wei Zhang, Sheng Cao, Jessica L Martin, Joachim D Mueller, Louis M Mansky
{"title":"Morphology and ultrastructure of retrovirus particles.","authors":"Wei Zhang,&nbsp;Sheng Cao,&nbsp;Jessica L Martin,&nbsp;Joachim D Mueller,&nbsp;Louis M Mansky","doi":"10.3934/biophy.2015.3.343","DOIUrl":null,"url":null,"abstract":"<p><p>Retrovirus morphogenesis entails assembly of Gag proteins and the viral genome on the host plasma membrane, acquisition of the viral membrane and envelope proteins through budding, and formation of the core through the maturation process. Although in both immature and mature retroviruses, Gag and capsid proteins are organized as paracrystalline structures, the curvatures of these protein arrays are evidently not uniform within one or among all virus particles. The heterogeneity of retroviruses poses significant challenges to studying the protein contacts within the Gag and capsid lattices. This review focuses on current understanding of the molecular organization of retroviruses derived from the sub-nanometer structures of immature virus particles, helical capsid protein assemblies and soluble envelope protein complexes. These studies provide insight into the molecular elements that maintain the stability, flexibility and infectivity of virus particles. Also reviewed are morphological studies of retrovirus budding, maturation, infection and cell-cell transmission, which inform the structural transformation of the viruses and the cells during infection and viral transmission, and lead to better understanding of the interplay between the functioning viral proteins and the host cell.</p>","PeriodicalId":7529,"journal":{"name":"AIMS Biophysics","volume":"2 3","pages":"343-369"},"PeriodicalIF":1.1000,"publicationDate":"2015-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3934/biophy.2015.3.343","citationCount":"52","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"AIMS Biophysics","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.3934/biophy.2015.3.343","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2015/8/18 0:00:00","PubModel":"Epub","JCR":"Q4","JCRName":"BIOPHYSICS","Score":null,"Total":0}
引用次数: 52

Abstract

Retrovirus morphogenesis entails assembly of Gag proteins and the viral genome on the host plasma membrane, acquisition of the viral membrane and envelope proteins through budding, and formation of the core through the maturation process. Although in both immature and mature retroviruses, Gag and capsid proteins are organized as paracrystalline structures, the curvatures of these protein arrays are evidently not uniform within one or among all virus particles. The heterogeneity of retroviruses poses significant challenges to studying the protein contacts within the Gag and capsid lattices. This review focuses on current understanding of the molecular organization of retroviruses derived from the sub-nanometer structures of immature virus particles, helical capsid protein assemblies and soluble envelope protein complexes. These studies provide insight into the molecular elements that maintain the stability, flexibility and infectivity of virus particles. Also reviewed are morphological studies of retrovirus budding, maturation, infection and cell-cell transmission, which inform the structural transformation of the viruses and the cells during infection and viral transmission, and lead to better understanding of the interplay between the functioning viral proteins and the host cell.

Abstract Image

Abstract Image

Abstract Image

逆转录病毒颗粒的形态和超微结构。
逆转录病毒的形态发生包括Gag蛋白和病毒基因组在宿主质膜上的组装,通过出芽获得病毒膜和包膜蛋白,并通过成熟过程形成核心。尽管在未成熟和成熟的逆转录病毒中,Gag和衣壳蛋白都以准晶结构组织,但这些蛋白质阵列的曲率在一个或所有病毒颗粒中显然是不均匀的。逆转录病毒的异质性对研究Gag和衣壳晶格内的蛋白质接触提出了重大挑战。本文综述了目前对逆转录病毒分子结构的认识,包括未成熟病毒颗粒的亚纳米结构、螺旋衣壳蛋白组装体和可溶性包膜蛋白复合物。这些研究提供了对维持病毒颗粒稳定性、灵活性和传染性的分子元素的深入了解。综述了逆转录病毒出芽、成熟、感染和细胞-细胞传播的形态学研究,这些研究为病毒和细胞在感染和病毒传播过程中的结构转化提供了信息,并有助于更好地了解功能病毒蛋白与宿主细胞之间的相互作用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
AIMS Biophysics
AIMS Biophysics BIOPHYSICS-
CiteScore
2.40
自引率
20.00%
发文量
16
审稿时长
8 weeks
期刊介绍: AIMS Biophysics is an international Open Access journal devoted to publishing peer-reviewed, high quality, original papers in the field of biophysics. We publish the following article types: original research articles, reviews, editorials, letters, and conference reports. AIMS Biophysics welcomes, but not limited to, the papers from the following topics: · Structural biology · Biophysical technology · Bioenergetics · Membrane biophysics · Cellular Biophysics · Electrophysiology · Neuro-Biophysics · Biomechanics · Systems biology
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信