Palmitoylation of the Bovine Foamy Virus Envelope Glycoprotein Is Required for Viral Replication

被引：6

作者：

Chai, Keli ^{[1
]}

Wang, Zhaohuan ^{[1
]}

Xu, Yali ^{[1
]}

Zhang, Junshi ^{[1
]}

Tan, Juan ^{[1
]}

Qiao, Wentao ^{[1
]}

机构：

[1] Nankai Univ, Coll Life Sci, Minist Educ, Key Lab Mol Microbiol & Technol, Tianjin 300071, Peoples R China

来源：

VIRUSES-BASEL | 2021年 / 13卷 / 01期

基金：

中国国家自然科学基金;

关键词：

bovine foamy virus; envelope glycoprotein; palmitoylation; BDHHC3; BDHHC20; membrane fusion; subviral particle; cell surface; replication;

D O I：

10.3390/v13010031

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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.

引用

页数：16

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