The preparation of P particle of the norovirus strain SZ9711 from China and its affinity analysis with human histo-blood group antigens in saliva.
- Author:
Miao JIN
1
;
Ya-Qing HE
;
Hui-Ying LI
;
Hong YANG
;
Hai-Long ZHANG
;
Rui QI
;
Xiao-Ke YANG
;
Shi-Song FANG
;
Ming TAN
;
Zhao-Jun DUAN
Author Information
- Publication Type:Journal Article
- MeSH: Blood Group Antigens; metabolism; Caliciviridae Infections; metabolism; virology; China; Humans; Norovirus; chemistry; genetics; metabolism; Protein Binding; Saliva; chemistry; metabolism; Viral Proteins; genetics; isolation & purification; metabolism
- From: Chinese Journal of Experimental and Clinical Virology 2010;24(1):5-7
- CountryChina
- Language:Chinese
-
Abstract:
OBJECTIVETo study the binding profile of NV strain SZ9711 (GII-4) with human histo-blood group antigens (HBGAs).
METHODSThe P domain-encoding fragment was amplified by RT-PCR from the stain SZ9711 and cloned into the pGEX-4T-1 vector. The recombinant fusion protein was expressed in E. coli and purified using the column Sepharose 4B. The P protein was released by thrombin cleavage. The binding of P particles of SZ9711 and VA387 with the HBGAs were measured by saliva-based EIA method.
RESULTSThe expression of the recombinant fusion protein was shown by the SDS-PAGE, in which a 38 x 10(3)-P protein was obtained. Saliva-based EIA revealed that the P particle of SZ9711 bound to HBGAs in saliva similar to that of the strain VA387 reported previously. It bound strongly to saliva of type A, B and O(secretor) but did not interact with saliva of type O(non-secretor). Noteworthy, binding ability of SZ9711 P particle to type A saliva was lower than that of the VA387 P particle.
CONCLUSIONThis is the first time that a P particle was prepared from a norovirus strain isolated in China and the binding ability of the P particle with HBGAs was analyzed. The result indicated the binding profile of the SZ9711 P particle was similar to that of VA387 reported previously. These data may be valuable in studying the relationship between noroviruses and their bindings to HGBA receptors.