Linear epitope binding antibodies against GII.3 Norovirus exhibit no histo-blood group antigens (HBGAs) blocking effects
Autor: | Xuhui Chen, Mingchen Wang, Zhaojie Yang, Yuqi Huo, Jinjin Liu, Lijun Zheng, Li Li, Shuhuan Ma, Jie Ma, Fukun Zhang, Wenhui Wang |
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Rok vydání: | 2019 |
Předmět: |
Genotype
viruses Guinea Pigs Biology Antibodies Virus Epitope Epitopes 03 medical and health sciences fluids and secretions Antigen Virology Blocking antibody Genetics medicine Animals Humans Binding site Molecular Biology 030304 developmental biology 0303 health sciences Binding Sites Linear epitope 030306 microbiology Norovirus virus diseases General Medicine biochemical phenomena metabolism and nutrition Trypsin In vitro Gastroenteritis Blood Group Antigens Capsid Proteins Rabbits Protein Binding Signal Transduction medicine.drug |
Zdroj: | Virus Genes. 55:280-289 |
ISSN: | 1572-994X 0920-8569 |
Popis: | Noroviruses are leading cause of acute gastroenteritis worldwide. In our previous study, we established an in vitro histo-blood group antigens (HBGAs) binding blockade assay against GII.3 Norovirus virus like particles (VLPs) with trypsin digestion. In this study, we characterized the blocking antibody binding site and epitope type (linear or conformational) by using hyperimmune sera produced against different antigens. VP1 from Jingzhou402 (GII.3, JZ402) strain was expressed by using pGEX-6p-1 expression vector and the insoluble proteins were purified for immunization in rabbit. Previously characterized chimeric VP1-assembled VLPs (GII.4-VP1/GII.3-P2) were used to immunize guinea pig. Peptides reactive with hyperimmune serum against VLPs derived from the VP1 of JZ402 strain were conjugated with BSA and used to immunize rabbits. Hyperimmune sera against above antigens and JZ402 and JZ403 strain-derived VLPs were used to compare their HBGAs blocking effects. Rabbit anti-GST-VP1 and BSA-peptide conjugated hyperimmune sera demonstrated no blocking effects against the binding of GII.3 and GII.4 NoV VLPs to salivary HBGAs. Guinea pig anti-GII.4-VP1/GII.3-P2 hyperimmune serum blocked the binding of trypsin cleaved GII.3 VLPs to salivary HBGAs with no or very weak blocking effects against the binding of GII.4 VLPs to salivary HBGAs. Our data indicated that HBGAs blocking antibodies primarily bound the P2 domain of GII.3 NoV VP1 and their binding epitopes were most probably conformation-dependent. |
Databáze: | OpenAIRE |
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