A glycoprotein B-neutralizing antibody structure at 2.8 Å uncovers a critical domain for herpesvirus fusion initiation

Herpesvirus virions have an outer lipid membrane dotted with glycoproteins that enable fusion with cell membranes to initiate entry and establish infection. Here the authors elucidate the structural mechanism of a neutralizing antibody derived from a patient infected by the herpesvirus varicella-zos...

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Main Authors: Stefan L. Oliver, Yi Xing, Dong-Hua Chen, Soung Hun Roh, Grigore D. Pintilie, David A. Bushnell, Marvin H. Sommer, Edward Yang, Andrea Carfi, Wah Chiu, Ann M. Arvin
Format: Article
Language:English
Published: Nature Publishing Group 2020-08-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-020-17911-0
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spelling doaj-29372bf848da493084861c63723dc16f2021-08-22T11:41:53ZengNature Publishing GroupNature Communications2041-17232020-08-0111111510.1038/s41467-020-17911-0A glycoprotein B-neutralizing antibody structure at 2.8 Å uncovers a critical domain for herpesvirus fusion initiationStefan L. Oliver0Yi Xing1Dong-Hua Chen2Soung Hun Roh3Grigore D. Pintilie4David A. Bushnell5Marvin H. Sommer6Edward Yang7Andrea Carfi8Wah Chiu9Ann M. Arvin10Department of Pediatrics, Stanford University School of MedicineGSK VaccinesStructural Biology, Stanford University School of MedicineDepartment of Biological Sciences, Institute of Molecular Biology & Genetics, Seoul National UniversityBioengineering, Stanford University School of MedicineStructural Biology, Stanford University School of MedicineDepartment of Pediatrics, Stanford University School of MedicineDepartment of Pediatrics, Stanford University School of MedicineGSK VaccinesBioengineering, Stanford University School of MedicineDepartment of Pediatrics, Stanford University School of MedicineHerpesvirus virions have an outer lipid membrane dotted with glycoproteins that enable fusion with cell membranes to initiate entry and establish infection. Here the authors elucidate the structural mechanism of a neutralizing antibody derived from a patient infected by the herpesvirus varicella-zoster virus and targeted to its fusogen, glycoprotein-B.https://doi.org/10.1038/s41467-020-17911-0
collection DOAJ
language English
format Article
sources DOAJ
author Stefan L. Oliver
Yi Xing
Dong-Hua Chen
Soung Hun Roh
Grigore D. Pintilie
David A. Bushnell
Marvin H. Sommer
Edward Yang
Andrea Carfi
Wah Chiu
Ann M. Arvin
spellingShingle Stefan L. Oliver
Yi Xing
Dong-Hua Chen
Soung Hun Roh
Grigore D. Pintilie
David A. Bushnell
Marvin H. Sommer
Edward Yang
Andrea Carfi
Wah Chiu
Ann M. Arvin
A glycoprotein B-neutralizing antibody structure at 2.8 Å uncovers a critical domain for herpesvirus fusion initiation
Nature Communications
author_facet Stefan L. Oliver
Yi Xing
Dong-Hua Chen
Soung Hun Roh
Grigore D. Pintilie
David A. Bushnell
Marvin H. Sommer
Edward Yang
Andrea Carfi
Wah Chiu
Ann M. Arvin
author_sort Stefan L. Oliver
title A glycoprotein B-neutralizing antibody structure at 2.8 Å uncovers a critical domain for herpesvirus fusion initiation
title_short A glycoprotein B-neutralizing antibody structure at 2.8 Å uncovers a critical domain for herpesvirus fusion initiation
title_full A glycoprotein B-neutralizing antibody structure at 2.8 Å uncovers a critical domain for herpesvirus fusion initiation
title_fullStr A glycoprotein B-neutralizing antibody structure at 2.8 Å uncovers a critical domain for herpesvirus fusion initiation
title_full_unstemmed A glycoprotein B-neutralizing antibody structure at 2.8 Å uncovers a critical domain for herpesvirus fusion initiation
title_sort glycoprotein b-neutralizing antibody structure at 2.8 å uncovers a critical domain for herpesvirus fusion initiation
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2020-08-01
description Herpesvirus virions have an outer lipid membrane dotted with glycoproteins that enable fusion with cell membranes to initiate entry and establish infection. Here the authors elucidate the structural mechanism of a neutralizing antibody derived from a patient infected by the herpesvirus varicella-zoster virus and targeted to its fusogen, glycoprotein-B.
url https://doi.org/10.1038/s41467-020-17911-0
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