Nonstructural protein 14 of PDCoV promotes complement C3 expression via the activation of p38-MAPK-C/EBP pathway

文献类型： 外文期刊

第一作者： Chen, Zhuoqi

作者： Chen, Zhuoqi;Fan, Liyuan;Shang, Hongqi;Xiao, Li;Wang, Wei;Guo, Rongli;Li, Jizong;Chen, Zhuoqi;Fan, Liyuan;Shang, Hongqi;Wang, Wei;Guo, Rongli;Li, Jizong;Li, Jizong;Li, Jizong;Li, Jizong;Li, Jizong;Zhong, Chunyan

作者机构： Jiangsu Acad Agr Sci, Inst Vet Med, Key Lab Vet Biol Engn & Technol, Minist Agr, Nanjing 210014, Peoples R China;Minist Sci & Technol, Jiangsu Key Lab Food Qual & Safety, State Key Lab Cultivat Base, Nanjing 210014, Peoples R China;Jiangsu Univ, Inst Life Sci, Sch Food & Biol Engn, Zhenjiang 212013, Peoples R China;Nanjing Agr Univ, Coll Vet Med, Nanjing 210095, Peoples R China;Yangzhou Univ, Jiangsu Coinnovat Ctr Prevent & Control Important, Yangzhou 225009, Peoples R China;GuoTai Taizhou Ctr Technol Innovat Vet Biol, Taizhou 225300, Peoples R China;Southwest Guizhou Vocat & Tech Coll Nationalities, Biol Engn Dept, Xingyi 562400, Peoples R China

关键词： PDCoV; C3; Nsp14; Complement; C/EBP-beta

期刊名称：VETERINARY MICROBIOLOGY （ 2023影响因子：2.4； 五年影响因子：2.6 ）

ISSN： 0378-1135

年卷期： 2024 年 295 卷

页码：

收录情况： SCI

摘要： Porcine deltacoronavirus (PDCoV) is an emergent enteric coronavirus, primarily inducing diarrhea in swine, particularly in nursing piglets, with the additional potential for zoonotic transmission to humans. Despite the significant impact of PDCoV on swine populations, its pathogenic mechanisms remain incompletely understood. Complement component 3 (C3) plays a pivotal role in the prevention of viral infections, however, there are no reports concerning the influence of C3 on the proliferation of PDCoV. In this study, we initially demonstrated that PDCoV is capable of activating the C3 and eliciting inflammatory responses. The overexpression of C3 significantly suppressed PDCoV replication, while inhibition of C3 expression facilitated PDCoV replication. We discovered that nonstructural proteins Nsp7, Nsp14, and M, considerably stimulated C3 expression, particularly Nsp14, through activation of the p38-MAPK-C/EBP-beta pathway. The N7-MTase constitutes a significant functional domain of the non-structural protein Nsp14, which is more obvious to upregulate C3. Furthermore, functional mutants of the N7-MTase domain suggested that the D44 and T135 of N7-Mtase constituted a pivotal amino acid site to promote C3 expression. This provides fresh insights into comprehending how the virus manipulates the host immune response and suggests potential antiviral strategies against PDCoV.

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