中国动物传染病学报2023，Vol.31Issue(5)：1-6,6.
血凝素蛋白145位潜在糖基化位点对H9N2禽流感病毒生物学特性的影响
Effect of the Potential Glycosylation Site at HA145 on the Biological Characteristics of H9N2 Avian Influenza Virus
摘要
Abstract
Previous studies have reported that the Avian influenza virus A/Chicken/Jiangxi/106/2012(H9N2,JX106)isolated from a broiler farm has a S to N mutation at amino acid position 145 of HA protein,which may produce a new potential glycosylation site in HA.In this study,reassort viruses rgJX106-HA145N and rgJX106-HA145S were rescued by reverse genetic system and used to investigate the effect of S145N substitution on viral growth kinetic,receptor affinity and pathogenicity in mice.We found that S145N mutation had no effect on the growth of the virus in both chicken embryos and A549 cells.The reassort virus rgJX106-HA145S had no glycosylation site at position 145 of HA protein but preferred to bind with α2,6-sialic acid receptors.In addition,mice inoculated with rgJX106-HA145S showed higher viral titers in the lungs than the rgJX106-HA145N at day 3 post infection.Moreover,the rgJX106-HA145S caused more significant weight loss in mice and induced higher cross-reactive antibodies.All results indicated that the glycosylation in HA had an important impact on humoral immunity.关键词
H9N2 AIV/潜在糖基化位点/病毒拯救/致病性Key words
H9N2 Avian influenza virus/glycosylation site/viral rescue/pathogenicity分类
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王娅娟,王飞,吴锦森,万志敏,邵红霞,钱琨,叶建强,秦爱建..血凝素蛋白145位潜在糖基化位点对H9N2禽流感病毒生物学特性的影响[J].中国动物传染病学报,2023,31(5):1-6,6.基金项目
国家重点研发计划(2017YFD0501100) （2017YFD0501100）
