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Pena-Francesch, M.* ; Vanoaica, L.D.* ; Zhu, G.F.* ; Stumpe, M.* ; Sankar, D.S.* ; Nowag, H.* ; Valencia-Camargo, A.D.* ; Hammerschmidt, W. ; Dengjel, J.* ; Ligeon, L.A.* ; Münz, C.*

The autophagy machinery interacts with EBV capsids during viral envelope release.

Proc. Natl. Acad. Sci. U.S.A. 120:e2211281120 (2023)
DOI PMC
Autophagy serves as a defense mechanism against intracellular pathogens, but several microorganisms exploit it for their own benefit. Accordingly, certain herpesviruses include autophagic membranes into their infectious virus particles. In this study, we analyzed the composition of purified virions of the Epstein-Barr virus (EBV), a common oncogenic γ-herpesvirus. In these, we found several components of the autophagy machinery, including membrane-associated LC3B-II, and numerous viral proteins, such as the capsid assembly proteins BVRF2 and BdRF1. Additionally, we showed that BVRF2 and BdRF1 interact with LC3B-II via their common protein domain. Using an EBV mutant, we identified BVRF2 as essential to assemble mature capsids and produce infectious EBV. However, BdRF1 was sufficient for the release of noninfectious viral envelopes as long as autophagy was not compromised. These data suggest that BVRF2 and BdRF1 are not only important for capsid assembly but together with the LC3B conjugation complex of ATG5-ATG12-ATG15L1 are also critical for EBV envelope release.
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Publication type Article: Journal article
Document type Scientific Article
Corresponding Author
Keywords Ebv ; Autophagy ; Viral Capsid Assembly ; Viral Envelope ; Xenophagy; Epstein-barr-virus; Extracellular Vesicles; Proteins; Replication; Infection; Blocks; Fusion; Roles; Motif; Flux
ISSN (print) / ISBN 0027-8424
e-ISSN 1091-6490
Journal Proceedings of the National Academy of Sciences of the United States of America
Quellenangaben Volume: 120, Issue: 34, Pages: , Article Number: e2211281120 Supplement: ,
Publisher National Academy of Sciences
Publishing Place 2101 Constitution Ave Nw, Washington, Dc 20418 Usa
Non-patent literature Publications
Reviewing status Peer reviewed
Institute(s) Research Unit Gene Vector (AGV)
Grants Novartis
Cancer Research Center Zurich
Swiss NSF
Vontobel Foundation
Roche
Swiss MS Society
Swiss Vaccine Research Institute
Sobek Foundation
HMZ ImmunoTargET of the University of Zurich
Cancer Research Switzerland
Forschungskredit of the University of Zurich