Antigenicity and Histo-blood Group Antigen-binding Characteristics of Human GⅡ.14 Norovirus VLPs
This study aimed to get the virus-like particles(VLPs)of human GⅡ.14 norovirus(NoV)and explore its binding characteristics with histo-blood group antigens(HBGAs).The VP1 protein of human GⅡ.14 NoV was expreesed by baculovirus system.VLPs were purified by ultracentrifugation and gel-filtration chromatography.Rabbit polyclonal antisera were generated by immunizing animals with GⅡ.14 VLPs.The function of polyclonal antibodies was verified by western blotting and enzyme-linked immunosorbent assay.The saliva-binding assay was carried out to detect the glycan-binding characteristics of human GⅡ.14 VLPs.Potential glycan binding sites of the GⅡ.14 P protein were analyzed by sequence alignment and structural comparison.The purified GⅡ.14 VP1 protein formed relatively uniform VLPs when observed by electron microscopy.Rabbit polyclonal antibodies could specifically bind to GⅡ.14 VLPs with no obvious cross-reactivity with other tested VLPs.GⅡ.14 VLPs bound well to human saliva of A/B/O/AB types according to the saliva-binding assay.Sequence and structural analyses showed that the simulated structure of the GⅡ.14 P protein was closest to GⅡ.9 P protein,and possessed similar potential glycan-binding sites to that of GⅡ.9 and the epidemic GⅡ.4.Our data indicate that GⅡ.14 has relatively broad binding characteristics to saliva.The potential glycan-binding mechanism of GⅡ.14 was illustrated through sequence alignment and structural comparison.Our results provide more evidence for the epidemic monitoring of NoVs of different genotypes.
NorovirusVirus-like particle(VLP)Histo-blood group antigen(HBGA)
万方数据
维普
