Journal of Infectious Disease and Pathology
Open Access

Research Article

Expression and Characterization of Capsid Proteins Derived from GII.17 and GII.7 Noroviruses

¹Wuhan Institute of Biological Products, Wuhan P. R. China

²The Sixth People’s Hospital of Zhengzhou, Zhengzhou P. R. China

^#These authors contributed equally

*Corresponding Author:

Zejun Wang
Wuhan Institute of Biological Products Co., Ltd. (WIBP)
No. 1 Golden Industrial Park Road
Zhengdian, Jiangxia Dist. Wuhan
430207, China
E-mail: wangzejun@sinopharm.com

Received date: July 26, 2016; Accepted date: September 09, 2016; Published date: September 20, 2016

Citation: Wan X, Wang W, Huo Y, Ling T, Ding L, et al. (2016) Expression and Characterization of Capsid Proteins Derived from GII.17 and GII.7 Noroviruses. J Emerg Infect Dis 1:113. doi:10.4172/2472-4998.1000113

Copyright: © 2016 Wan X, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Objective: Noroviruses (NoVs) are the leading cause of non-bacterial gastroenteritis worldwide and genogroup II, genotype 4 variants have been responsible for the majority of outbreaks reported. In winter 2014-15, the transient burst outbreaks caused by a new GII.17 variant that differed from previous strains was observed in several countries. In this study, major capsid proteins derived from GII.17 and GII.7 NoVs were expressed in sf9 cells and used to produce hyperimmune sera in rabbits for characterization of GII.17 and GII7 NoV Virus like particles (VLPs).

Methods: Baculovirus-insect cell expression system was used to assemble NoV VLPs. Salivary HBGA-viruslike particle (VLP) binding and binding blockade assays were performed.

Results: High expression levels were observed for both capsid proteins and expression led to successful assembly of VLPs. CsCl density gradient centrifugation indicated presence of two bands for both VLPs and SDS-PAGE analysis of these two bands showed contradictory ratio of the full-length and truncated capsid proteins. Both VLPs bound to salivary HBGAs derived from blood type A, B, AB and O individuals. In vitro HBGA-VLP binding blockade assay using hyperimmune sera against multiple genotypes, including current pandemic Sydney 2012 GII.4, GI.2, GII.7 and GII.17 VLPs demonstrated absence of blocking antibodies against the binding of GII.17 and GII.7 VLPs to salivary HBGAs.

Conclusion: The expression of GII.17 and GII.7 capsid proteins and VLP assembling allowed the antigenic comparison of different recombinant NoVs.

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