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The CP123L protein of African swine fever virus is a membrane-associated, palmitoylated protein required for viral replication

文献类型: 外文期刊

作者: Guan, Xiangyu;Wang, Tao;Gao, Yuxuan;Zhai, Huanjie;Jiang, Fengwei;Hou, Qinghe;Yang, Xiaoke;Wu, Hongxia;Li, Lian-Feng;Luo, Yuzi;Li, Su;Sun, Yuan;Qiu, Hua-Ji;Li, Yongfeng

作者机构:

关键词: palmitoylation;African swine fever virus;CP123L protein;replication;budding

期刊名称: JOURNAL OF VIROLOGY

ISSN: 0022-538X

年卷期: 2025 年

页码:

收录情况: SCIE(2024版)

摘要: African swine fever (ASF) is a highly contagious and often lethal disease caused by African swine fever virus (ASFV) in pigs. Protein palmitoylation is a prevalent posttranslational lipid modification that can modulate viral replication. In this study, we investigated the palmitoylation of ASFV proteins. The results revealed that the CP123L protein (pCP123L) of ASFV was palmitoylated at the cysteine residue at position 18 (C18). To further elucidate the functional significance of this posttranslational modification, abolishing palmitoylation through a cysteine-to-serine mutation at C18 (C18S) of pCP123L (pCP123L/C18S) or treatment with 2-bromopalmitate (2-BP), a palmitoylation inhibitor, led to altered cytomembrane localization and migration rate of pCP123L. Furthermore, depalmitoylation achieved through 2-BP treatment significantly suppressed ASFV replication and exerted a profound impact on virus budding. Remarkably, blocking pCP123L palmitoylation via the C18S mutation resulted in decreased replication of ASFV. Our study represents the first evidence for the presence of palmitoylation in ASFV proteins and underscores its crucial role in viral replication.

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