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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2020-08-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-020-17911-0 |
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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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