ACTA VETERINARIA ET ZOOTECHNICA SINICA ›› 2016, Vol. 47 ›› Issue (2): 325-330.doi: 10.11843/j.issn.0366-6964.2016.02.015

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Expression of the P Dimer of Rabbit Hemorrhagic Disease Virus Capsid Protein and Analysis of Its Binding Ability to Receptor

HU Bo,FAN Zhi-yu,WANG Fang*,WEI Hou-jun,SONG Yan-hua,QIU Ru-long,XU Wei-zhong,XUE Jia-bin   

  1. (Institute of Veterinary Medicine,Jiangsu Academy of Agricultural Sciences/Key Laboratory of Veterinary Biological Engineering and Technology of Ministry of Agriculture /National Center for Engineering Research of Veterinary Bio-products,Nanjing 210014,China)
  • Received:2015-06-20 Online:2016-02-23 Published:2016-02-23

Abstract:

Rabbit hemorrhagic disease virus (RHDV) is a member of the Caliciviridae family (Lagovirus genus).Similar to human norovirus (CaliciviridaeNorovirus genus),RHDV binds histo-blood group antigens (HBGAs) and this is thought to be important for infection.The aim of this study was to determine whether the P domain of RHDV capsid protein (VP60) could form dimers and to analyze its binding ability to HBGAs receptor.The P domain gene containing hinge (HP) was amplified and cloned into pET-28a (+) expression vector and introduced into Escherichia coli BL21 (DE3).The recombinant HP protein,confirmed by SDS-PAGE and Western blot,was effectively expressed in form of inclusion bodies by inducing with IPTG.The recombinant protein was then purified with HisTrap affinity chromatography,which could form dimers after purification.The HBGAs binding assay showed that the P domain bound H type HBGA with the same patterns as those of the intact viral capsids.Further structural studies with P domain are needed in order to better understand the HBGA binding mechanisms and virus-receptor interaction.

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