- VernacularTitle:GⅡ.5型诺如病毒衣壳蛋白糖受体结合特征分析
- Author:
Xin CONG
1
Author Information
- Publication Type:Journal Article
- Keywords: Norovirus(NoV); Capsid proteins; Saliva; Glycan; Binding characteristics; Molecular model
- From: Chinese Journal of Biologicals 2026;39(03):277-281+288
- CountryChina
- Language:Chinese
- Abstract: ObjectiveTo analyze the glycan receptor binding characteristics of capsid proteins of GⅡ.5 norovirus(NoV) in order to lay a foundation for the development of antiviral drugs and vaccines for NoV.MethodsThe P proteins of GⅡ.5 N490 and GⅡ.5 12X were expressed in prokaryotic system respectively, purified using glutathione affinity chromatography, and then the binding characteristics of P proteins with saliva and glycan were detected by ELISA. The structure of two GⅡ.5 strains was modeled and the binding amino acids between the P protein and glycan were analyzed based on the epidemic GⅡ.17 KW308.ResultsThe relative molecular mass of the both P proteins of GⅡ.5 N490 and GⅡ.5 12X was 61 000,which were expressed in soluble from in the supernatant, and the purified concentration was 0. 2 mg/mL. The P proteins of two GⅡ.5 strains could bind to most of A, B, O secretory and non-secretory saliva. The P protein of GⅡ.5 N490 exhibited binding to H disaccharide, while the P protein of GⅡ.5 12X showed specific binding to H disaccharide and B trisaccharide. In addition, the model of two GⅡ.5 strains displayed a conformation similar to that of GⅡ.17 KW308. Among the six amino acid sites interacting with glycan, Arg349, Asp378, Gly443 of GⅡ.5 N490 and GⅡ.5 12X were the same as those of G Ⅱ.17 KW308, while Asn375, Glu380 and Phe444 were different from those of G Ⅱ.17 KW308.ConclusionThe two strains of G Ⅱ. 5 exhibit similar binding characteristics in saliva binding patterns with P proteins and both have a wide susceptible population, while the glycan binding patterns are slightly different.


