Comprehensive characterization of a major capsid protein derived from a documented GII.6 norovirus strain

作者：Zheng, Lijun; Wang, Wenhui; Liu, Jinjin; Huo, Yuqi^*; Qin, Chuan^*; Wang, Mingchen; Shen, Shuo

来源：Archives of Virology, 2017, 162(12): 3863-3868.

DOI：10.1007/s00705-017-3537-4

• Noroviruses
• Major capsid protein
• Truncated protein
• Packaging signal sequence
• Blocking antibody

In this study, we successfully produced VLPs derived from full-length or chimeric VP1 of a documented GII.6 strain. Trypsin digestion of purified VLPs led to total cleavage of VP1, while the integrity of assembled VLPs was not affected. In vitro VLP-histo-blood group antigen (HBGA) binding and binding blockade assays indicated that trypsin digestion enhanced the binding of GII.6 VLPs to salivary HBGAs and that this binding could only be blocked by serum produced against a homologous strain. The data regarding the assembly, morphology and binding patterns of GII.6 NoV VLPs presented here might be useful for further study of GII.6 NoVs.

• 出版日期2017-12
• 单位郑州大学