HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Supplementary table and figures All Versions of this Article: vir.0.015081-0v1 90/12/2952    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via CrossRef Google Scholar Articles by Chen, L. Articles by Chen, J. PubMed PubMed Citation Articles by Chen, L. Articles by Chen, J. Agricola Articles by Chen, L. Articles by Chen, J.

Minor structural protein VP2 in rabbit hemorrhagic disease virus downregulates the expression of the viral capsid protein VP60

Guangqing Liu^1,

¹ Institute of Virology and Biotechnology, Zhejiang Academy of Agriculture Sciences, Hangzhou 310021, PR China
² College of Chemistry and Life Sciences, Zhejiang Normal University, Jinhua 321004, PR China

Correspondence
Guangqing Liu
wg6810{at}sina.com
Jianping Chen
jpchen2001{at}yahoo.com.cn

Rabbit hemorrhagic disease virus (RHDV) has two structural proteins: the major capsid protein VP60 and the minor capsid protein VP2. VP2 is speculated to play an important role in the virus life cycle. To investigate the effect of VP2 on VP60 expression, three types of experiment (baculovirus–insect cell system, mammalian–luciferase assay system and in vitro coupled transcription/translation system) were used to express VP60 alone or co-expressed with VP2. Both forms of VP60 were able to form virus-like particles in insect cells. Western blot analysis and dual-luciferase assays demonstrated that the presence of VP2 results in downregulation of the expression of VP60 in vivo. Real-time RT-PCR of mRNA levels showed that downregulation of VP60 occurs at the transcriptional level. The ability of the viral minor structural protein VP2 to regulate capsid protein levels may contribute to effective virus infection.

Present address: Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai 200241, PR China.

A supplementary table showing primer sequences and three supplementary figures are available with the online version of this paper.