PuSH - Publikationsserver des Helmholtz Zentrums München

Export: TXT Text RIS Endnote (RIS) BIB BibTeX
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)
Verlagsversion DOI PMC
Open Access Hybrid
Creative Commons Lizenzvertrag
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.
Impact Factor
Scopus SNIP
Altmetric
11.100
0.000
Tags
Anmerkungen
Besondere Publikation
Auf Hompepage verbergern

Zusatzinfos bearbeiten
Eigene Tags bearbeiten
Privat
Eigene Anmerkung bearbeiten
Privat
Auf Publikationslisten für
Homepage nicht anzeigen
Als besondere Publikation
markieren
Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Ebv ; Autophagy ; Viral Capsid Assembly ; Viral Envelope ; Xenophagy; Epstein-barr-virus; Extracellular Vesicles; Proteins; Replication; Infection; Blocks; Fusion; Roles; Motif; Flux
Sprache englisch
Veröffentlichungsjahr 2023
HGF-Berichtsjahr 2023
ISSN (print) / ISBN 0027-8424
e-ISSN 1091-6490
Zeitschrift Proceedings of the National Academy of Sciences of the United States of America
Quellenangaben Band: 120, Heft: 34, Seiten: , Artikelnummer: e2211281120 Supplement: ,
Verlag National Academy of Sciences
Verlagsort 2101 Constitution Ave Nw, Washington, Dc 20418 Usa
Begutachtungsstatus Peer reviewed
Institut(e) Research Unit Gene Vector (AGV)
POF Topic(s) 30203 - Molecular Targets and Therapies
Forschungsfeld(er) Immune Response and Infection
PSP-Element(e) G-501500-001
Förderungen 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
DOI 10.1073/pnas.2211281120
WOS ID 001117389900001
Scopus ID 85168809081
PubMed ID 37579175
Erfassungsdatum 2023-10-06
[➜Korrektur melden]