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Capsid assembly is regulated by amino acid residues asparagine 47 and 48 in the VP2 protein of porcine parvovirus

文献类型： 外文期刊

作者： Wang, Jucai 1 ; Liu, Yunchao 1 ; Chen, Yumei 3 ; Zhang, Teng 1 ; Wang, Aiping 3 ; Wei, Qiang 1 ; Liu, Dongmin 4 ; Wang, F 1 ;

作者机构： 1.Henan Acad Agr Sci, Henan Prov Key Lab Anim Immunol, Zhengzhou 450002, Peoples R China

2.Henan Agr Univ, Coll Anim Sci & Vet Med, Zhengzhou 450002, Peoples R China

3.Zhengzhou Univ, Sch Life Sci, Zhengzhou 450001, Peoples R China

4.Henan Zhongze Biol Engn Co Ltd, Zhengzhou, Peoples R China

5.Yangzhou Univ, Jiangsu Co, Innovat Ctr Prevent & Control Important Anim Infe, Yangzhou, Jiangsu, Peoples R China

关键词： Porcine parvovirus; Capsid assembly; 47Asn; 48Asn; VP2 macromolecular polymers

期刊名称：VETERINARY MICROBIOLOGY （ 影响因子：3.293； 五年影响因子：3.599 ）

ISSN： 0378-1135

年卷期： 2021 年 253 卷

页码：

收录情况： SCI

摘要： Porcine parvovirus (PPV) is a major cause of reproductive failure in swine and has caused substantial losses throughout the world. Viral protein 2 (VP2) of PPV is a major structural protein that can self-assemble into virus-like particles (VLP) with hemagglutination (HA) activity. In order to identify the essential residues involved in the mechanism of capsid assembly and to further understand the function of HA, we analyzed a series of deletion mutants and site-directed mutations within the N-terminal of VP2 using the Escherichia coli system. Our results showed that deletion of the first 47 amino acids from the N-terminal of the VP2 protein did not affect capsid assembly, and further truncation to residue 48 Asparagine (Asn, N) caused detrimental effects. Site-directed mutagenesis experiments demonstrated that residue 47Asn reduced the assembly efficiency of PPV VLP, while residue 48Asn destroyed the stability, hemagglutination, and self-assembly characteristics of the PPV VP2 protein. Results from native PAGE inferred that macromolecular polymers were critical intermediates of the VP2 protein during the capsid assembly process. Site-directed mutation at 48Asn did not affect the ability of monomers to form into oligomers, but destroyed the ability of oligomers to assemble into macromolecular particles, influencing both capsid assembly and HA activity. Our findings provide valuable information on the mechanisms of PPV capsid assembly and the possibility of chimeric VLP vaccine development by replacing the first 47 amino acids at the N-terminal of the VP2 protein.

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