Palmitoylation of the Bovine Foamy Virus Envelope Glycoprotein Is Required for Viral Replication
Autor: | Junshi Zhang, Zhaohuan Wang, Juan Tan, Keli Chai, Wentao Qiao, Yali Xu |
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Jazyk: | angličtina |
Rok vydání: | 2020 |
Předmět: |
0301 basic medicine
replication viruses membrane fusion lcsh:QR1-502 Cattle Diseases envelope glycoprotein Context (language use) Virus Replication BDHHC3 Virus Article lcsh:Microbiology Cell Line 03 medical and health sciences Palmitoylation Viral envelope Viral Envelope Proteins Virology Animals palmitoylation BDHHC20 Cells Cultured Virus Release chemistry.chemical_classification 030102 biochemistry & molecular biology Chemistry Cell Membrane Lipid bilayer fusion bovine foamy virus Virus Internalization Cell biology Protein Transport 030104 developmental biology Infectious Diseases cell surface Membrane protein Viral replication Viral Envelope Spumavirus Cattle subviral particle Glycoprotein Protein Processing Post-Translational Retroviridae Infections |
Zdroj: | Viruses Volume 13 Issue 1 Viruses, Vol 13, Iss 31, p 31 (2021) |
ISSN: | 1999-4915 |
DOI: | 10.3390/v13010031 |
Popis: | Membrane proteins of enveloped viruses have been reported to undergo palmitoylation, a post-translational modification often having a critical role in the function of these viral proteins and hence viral replication. In this study, we report that the foamy virus (FV) envelope (Env) glycoprotein is palmitoylated. Specifically, we found that bovine foamy virus (BFV) Env (BEnv) is palmitoylated at amino acid positions C58 and C59 by BDHHC3 and BDHHC20 in a DHHC motif-dependent manner. In addition, mutations C58S and C58/59S significantly decrease cell surface expression of BEnv, subviral particle (SVP) egress, and its membrane fusion activity, thus ultimately inhibiting BFV replication. The C59S mutation exerts a minor effect in this regard. Taken together, these data demonstrate that the function of BEnv in the context of BFV replication is under the regulation of palmitoylation. |
Databáze: | OpenAIRE |
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