- Author:
Jian Fang ZHOU
1
;
Shu Mei ZOU
;
Zi LI
;
Min WANG
;
Jie DONG
;
Jun Feng GUO
;
He Jiang WEI
;
Le Ying WEN
;
Hong XU
;
Yue Long SHU
Author Information
- Publication Type:Journal Article
- MeSH: Adaptation, Biological; Animals; Chickens; China; epidemiology; Hemagglutination Tests; Humans; Influenza A Virus, H1N1 Subtype; metabolism; Influenza, Human; epidemiology; Polysaccharides; metabolism; Receptors, Cell Surface; metabolism; Receptors, Virus; metabolism; Sialic Acids; metabolism
- From: Biomedical and Environmental Sciences 2012;25(1):104-108
- CountryChina
- Language:English
-
Abstract:
OBJECTIVEBoth the 2, 6 linkage and its topology on target cells are critical for the recognition by human influenza virus. The binding preference of avian flu virus H5N1 HA to the 2, 3-linked sialylated glycans is considered the major factor limiting its efficient infection and transmission in humans. To monitor potential adaptation of H5N1 virus in human population, the surveillance of receptor-binding specificity was undertaken in China.
METHODSThe binding specificity of 32 human H5N1 virus strains isolated from 2003 to 2009 was tested by 2, 3-specific sialidase-treated chicken red blood cell (CRBC) agglutination assay and a solid-phase direct binding assay with synthetic sialylglycopolymers.
RESULTSDual binding preference to 2, 3 and 2, 6-glycans were found in two strains: A/Guangdong/1/06 (A/GD/1/06) and A/Guangxi/1/08 (A/GX/1/08). Though minor effect of short-2, 6-binding was detected in A/GX/1/08 at a low virus titer, both showed high affinity to the oligosaccharide at a high load. Notably both are of the long-2, 6-recognition, with the same topology as that of human H1N1 and H3N2 viruses.
CONCLUSIONThe findings suggest that human H5N1 virus in China likely acquired the potential human-adaptation ability. Further research and surveillance on receptor-binding specificity of H5N1 viruses are required.