Molecular basis of EphA2 recognition by gHgL from gammaherpesviruses

EphA2 is the specific entry receptor for both human γ-herpesviruses Kaposi sarcoma associated herpesvirus (KSHV) and Epstein-Barr virus (EBV). Here, the authors present the crystal structures of the EphA2 ligand binding domain (LBD) bound to the viral glycoprotein gHgL from EBV and KSHV and further...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Chao Su, Lili Wu, Yan Chai, Jianxun Qi, Shuguang Tan, George F. Gao, Hao Song, Jinghua Yan
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/ac26222e07064a76b8a070ea9eb86d83
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:ac26222e07064a76b8a070ea9eb86d83
record_format	dspace
spelling	oai:doaj.org-article:ac26222e07064a76b8a070ea9eb86d832021-12-02T14:16:24ZMolecular basis of EphA2 recognition by gHgL from gammaherpesviruses10.1038/s41467-020-19617-92041-1723https://doaj.org/article/ac26222e07064a76b8a070ea9eb86d832020-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-19617-9https://doaj.org/toc/2041-1723EphA2 is the specific entry receptor for both human γ-herpesviruses Kaposi sarcoma associated herpesvirus (KSHV) and Epstein-Barr virus (EBV). Here, the authors present the crystal structures of the EphA2 ligand binding domain (LBD) bound to the viral glycoprotein gHgL from EBV and KSHV and further analyse EphA2 gHgL interactions with mutagenesis experiments in cell-based fusion assays and suggest that other animal γ-herpesviruses could also use EphA2 as an entry receptor.Chao SuLili WuYan ChaiJianxun QiShuguang TanGeorge F. GaoHao SongJinghua YanNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Chao Su Lili Wu Yan Chai Jianxun Qi Shuguang Tan George F. Gao Hao Song Jinghua Yan Molecular basis of EphA2 recognition by gHgL from gammaherpesviruses
description	EphA2 is the specific entry receptor for both human γ-herpesviruses Kaposi sarcoma associated herpesvirus (KSHV) and Epstein-Barr virus (EBV). Here, the authors present the crystal structures of the EphA2 ligand binding domain (LBD) bound to the viral glycoprotein gHgL from EBV and KSHV and further analyse EphA2 gHgL interactions with mutagenesis experiments in cell-based fusion assays and suggest that other animal γ-herpesviruses could also use EphA2 as an entry receptor.
format	article
author	Chao Su Lili Wu Yan Chai Jianxun Qi Shuguang Tan George F. Gao Hao Song Jinghua Yan
author_facet	Chao Su Lili Wu Yan Chai Jianxun Qi Shuguang Tan George F. Gao Hao Song Jinghua Yan
author_sort	Chao Su
title	Molecular basis of EphA2 recognition by gHgL from gammaherpesviruses
title_short	Molecular basis of EphA2 recognition by gHgL from gammaherpesviruses
title_full	Molecular basis of EphA2 recognition by gHgL from gammaherpesviruses
title_fullStr	Molecular basis of EphA2 recognition by gHgL from gammaherpesviruses
title_full_unstemmed	Molecular basis of EphA2 recognition by gHgL from gammaherpesviruses
title_sort	molecular basis of epha2 recognition by ghgl from gammaherpesviruses
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/ac26222e07064a76b8a070ea9eb86d83
work_keys_str_mv	AT chaosu molecularbasisofepha2recognitionbyghglfromgammaherpesviruses AT liliwu molecularbasisofepha2recognitionbyghglfromgammaherpesviruses AT yanchai molecularbasisofepha2recognitionbyghglfromgammaherpesviruses AT jianxunqi molecularbasisofepha2recognitionbyghglfromgammaherpesviruses AT shuguangtan molecularbasisofepha2recognitionbyghglfromgammaherpesviruses AT georgefgao molecularbasisofepha2recognitionbyghglfromgammaherpesviruses AT haosong molecularbasisofepha2recognitionbyghglfromgammaherpesviruses AT jinghuayan molecularbasisofepha2recognitionbyghglfromgammaherpesviruses
_version_	1718391685655822336

Molecular basis of EphA2 recognition by gHgL from gammaherpesviruses

Ejemplares similares