Structure of Epstein-Barr virus tegument protein complex BBRF2-BSRF1 reveals its potential role in viral envelopment

Epstein-Barr virus (EBV) tegument proteins BBRF2 and BSRF1 have been suggested to form a hetero-complex. Here, He et al. provide the crystal structures of BBRF2 alone and in complex with BSRF1 and suggest that the complex tethers EBV nucleocapsids to the Golgi membrane, facilitating secondary envelo...

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Autores principales:	Hui-Ping He, Meng Luo, Yu-Lu Cao, Yu-Xin Lin, Hua Zhang, Xiao Zhang, Jun-Ying Ou, Bing Yu, Xiaoxue Chen, Miao Xu, Lin Feng, Mu-Sheng Zeng, Yi-Xin Zeng, Song Gao
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/64c685915d9748f7983479d521b37080
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spelling	oai:doaj.org-article:64c685915d9748f7983479d521b370802021-12-02T15:33:31ZStructure of Epstein-Barr virus tegument protein complex BBRF2-BSRF1 reveals its potential role in viral envelopment10.1038/s41467-020-19259-x2041-1723https://doaj.org/article/64c685915d9748f7983479d521b370802020-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-19259-xhttps://doaj.org/toc/2041-1723Epstein-Barr virus (EBV) tegument proteins BBRF2 and BSRF1 have been suggested to form a hetero-complex. Here, He et al. provide the crystal structures of BBRF2 alone and in complex with BSRF1 and suggest that the complex tethers EBV nucleocapsids to the Golgi membrane, facilitating secondary envelopment.Hui-Ping HeMeng LuoYu-Lu CaoYu-Xin LinHua ZhangXiao ZhangJun-Ying OuBing YuXiaoxue ChenMiao XuLin FengMu-Sheng ZengYi-Xin ZengSong GaoNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Hui-Ping He Meng Luo Yu-Lu Cao Yu-Xin Lin Hua Zhang Xiao Zhang Jun-Ying Ou Bing Yu Xiaoxue Chen Miao Xu Lin Feng Mu-Sheng Zeng Yi-Xin Zeng Song Gao Structure of Epstein-Barr virus tegument protein complex BBRF2-BSRF1 reveals its potential role in viral envelopment
description	Epstein-Barr virus (EBV) tegument proteins BBRF2 and BSRF1 have been suggested to form a hetero-complex. Here, He et al. provide the crystal structures of BBRF2 alone and in complex with BSRF1 and suggest that the complex tethers EBV nucleocapsids to the Golgi membrane, facilitating secondary envelopment.
format	article
author	Hui-Ping He Meng Luo Yu-Lu Cao Yu-Xin Lin Hua Zhang Xiao Zhang Jun-Ying Ou Bing Yu Xiaoxue Chen Miao Xu Lin Feng Mu-Sheng Zeng Yi-Xin Zeng Song Gao
author_facet	Hui-Ping He Meng Luo Yu-Lu Cao Yu-Xin Lin Hua Zhang Xiao Zhang Jun-Ying Ou Bing Yu Xiaoxue Chen Miao Xu Lin Feng Mu-Sheng Zeng Yi-Xin Zeng Song Gao
author_sort	Hui-Ping He
title	Structure of Epstein-Barr virus tegument protein complex BBRF2-BSRF1 reveals its potential role in viral envelopment
title_short	Structure of Epstein-Barr virus tegument protein complex BBRF2-BSRF1 reveals its potential role in viral envelopment
title_full	Structure of Epstein-Barr virus tegument protein complex BBRF2-BSRF1 reveals its potential role in viral envelopment
title_fullStr	Structure of Epstein-Barr virus tegument protein complex BBRF2-BSRF1 reveals its potential role in viral envelopment
title_full_unstemmed	Structure of Epstein-Barr virus tegument protein complex BBRF2-BSRF1 reveals its potential role in viral envelopment
title_sort	structure of epstein-barr virus tegument protein complex bbrf2-bsrf1 reveals its potential role in viral envelopment
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/64c685915d9748f7983479d521b37080
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Structure of Epstein-Barr virus tegument protein complex BBRF2-BSRF1 reveals its potential role in viral envelopment

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