Molecular evolution of hemagglutinin gene of H9N2 subtype of avian influenza virus
10.3760/cma.j.cn112866-20210521-00084
- VernacularTitle:H9N2亚型禽流感病毒血凝素基因的分子进化分析
- Author:
Libin YOU
1
;
Ying ZHU
;
Naipeng KAN
;
Jinzhang WANG
Author Information
1. 福建省疾病预防控制中心 福建省人兽共患病研究重点实验室，福州 350001
- Keywords:
H9N2;
Avian influenza virus;
Hemagglutinin(HA);
Genetic evolution
- From:
Chinese Journal of Experimental and Clinical Virology
2021;35(5):581-586
- CountryChina
- Language:Chinese
-
Abstract:
Objective:We attempted to investigate the variation of amino acids and molecular evolution trend of hemagglutinin(HA) genes of H9N2 avian influenza virus (AIV).Methods:In this study, we collected and aligned HA sequences of H9N2 AIV that submitted before April 2020 in the EpiFlu database. Then we analyzed the amino acid differences in the key sites of HA gene in bioinformatics method, including receptor binding sites, cleavage sites and glycosylation sites.Results:84.92% sequences have glutamine(Q) at the HA226 site in place of leucine(L) 84.75% sequences from avian and 72.97% sequences from mammals contained such HA-Q226 L mutation. 96.26% sequences still maintained the characteristics of low pathogenic AIV at the cleavage site of HA gene, except that 180 sequences from avian that two basic amino acids were inserted. Introducing one or two potential glycosylation sites were observed in 58.68% HA sequences, while loss of glycosylation site at HA210-212 in 66.44% sequences.Conclusions:The key protein receptor binding sites of the HA gene of H9N2 AIV showed obvious trends to binding human receptor. It revealed H9N2 AIV′s increasing adaptation to mammals. The cleavage sites and glycoylation sites of HA protein have a mutation tendency of characteristics of highly pathogenic AIV.
