Feline calicivirus VP2 is involved in the self-assembly of the capsid protein into virus-like particles

被引：21

作者：

Di Martino, B. ^{[1
]}

Marsilio, F. ^{[1
]}

机构：

[1] Univ Teramo, Dept Sci Biomed Comparate, I-64100 Teramo, Italy

来源：

RESEARCH IN VETERINARY SCIENCE | 2010年 / 89卷 / 02期

关键词：

FCV; VP1; VP2; Baculovirus system; VLPs; Morphology; NONSTRUCTURAL POLYPROTEIN; PRECURSOR PROTEIN; IDENTIFICATION; EXPRESSION; ORF3; POLYPEPTIDE; MAP;

D O I：

10.1016/j.rvsc.2010.03.011

中图分类号：

S85 [动物医学（兽医学）];

学科分类号：

0906 ;

摘要：

Feline calicivirus (FCV) is considered the most common upper respiratory tract disease (URTD) associated pathogen in cats. We previously expressed FCV VP1 capsid protein in insect cells by baculovirus system and we observed that this protein self-assemble into virus-like particles (VLPs) different in size and lacking the typical cup-like depressions of caliciviruses. In the present study, VP1 and the small basic structural protein VP2 of FCV were individually expressed by baculovirus system. Coinfection of insect cells with both recombinant viruses resulted in VP1 and VP2 self-assembly to form depressions similar to native capsids in size and appearance, demonstrating that VP2 interacts with the NMI protein in the formation of VLPs. (C) 2010 Elsevier Ltd. All rights reserved.

引用

页码：279 / 281

页数：3

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