湖北农业科学 ›› 2020, Vol. 59 ›› Issue (7): 212-217.doi: 10.14088/j.cnki.issn0439-8114.2020.07.044

• 生物工程 • 上一篇    

低致病性与高致病性H7N9亚型禽流感病毒分子特征及受体结合能力分析

薛玉涵1,2, 任助2, 商雨2, 唐国毅2, 贾妙妙2, 鲁岳峰2, 李琼琼2, 李慧敏2, 罗青平2, 温国元2, 潘兹书1, 赵宗正2   

  1. 1.武汉大学生命科学学院,武汉430072;
    2.湖北省农业科学院畜牧兽医研究所,武汉430064
  • 收稿日期:2019-04-04 发布日期:2020-06-28
  • 通讯作者: 赵宗正,助理研究员,(电子信箱)329517286@qq.com。
  • 作者简介:薛玉涵(1994-),女,山东泰安人,在读硕士研究生,研究方向为禽流感病毒,(电话)17671783952(电子信箱)490307914@qq.com;
  • 基金资助:
    国家重点研发计划(2016YFD0500202-2,2017YFD0501104-4); 国家现代农业产业技术体系建设专项资金(CARS-43-G11); 湖北省技术创新重大项目(2017ABA138)

Analysis of molecular characteristics and receptor-binding ability of low pathogenic and highly pathogenic H7N9 AIV subtype avian influenza virus

XUE Yu-han1,2, REN Zhu2, SHANG Yu2, TANG Guo-yi2, JIA Miao-miao2, LU Yue-feng2, LI Qiong-qiong2, LI Hui-min2, LUO Qing-ping2, WEN Guo-yuan2, PAN Zi-shu1, ZHAO Zong-zheng2   

  1. 1. College of Life Sciences,Wuhan University,Wuhan 430072,China;
    2. Institute of Animal Husbandry and Veterinary,Hubei Academy of Agricultural Sciences,Wuhan 430064,China
  • Received:2019-04-04 Published:2020-06-28

摘要: 对2017年从鸡病料中分离到的2株H7N9亚型禽流感病毒(Avian influenza virus,AIV)A/chicken/Hubei/093/2017(H7N9)和A/chicken/Hubei/207/2017(H7N9)(CK93和CK207)进行了全基因组测序。对血凝素(Hemagglutinin,HA)和神经氨酸酶(Neuraminidase,NA)序列保守性、HA糖基化位点、NA耐药位点和6个内部基因的关键氨基酸位点进行了分析,同时测定了2株毒株的受体结合能力。结果显示,CK93毒株HA裂解位点为PEIPKGR↓GLF,为低致病性AIV特征;而CK207毒株裂解位点为PKPKRTAR↓GLF,为高致病性AIV特征。HA第226位氨基酸在CK93毒株为亮氨酸(226L),而在CK207毒株为谷氨酰胺(226Q)。但受体结合能力测定发现,CK93和CK207都具有结合α-2,3唾液酸受体和α-2,6唾液酸受体的特性,说明Q226L并非影响病毒受体结合特性的决定性因素。本研究结果提示应加强对H7N9亚型禽流感病毒变异监测预防其突变可能造成流行的风险。

关键词: H7N9亚型禽流感病毒, 分子特征分析, 受体结合特性

Abstract: Two H7N9 subtype avian influenza viruses (AIV) isolated from chicken pathological material in Hubei Province, A/chicken/Hubei/093/2017(H7N9) and A/chicken/Hubei/207/2017(H7N9) (with CK93 and CK207 as their abbreviation, respectively) were analyzed for whole-genome sequencing. The hemagglutinin (HA) and neuraminidase (NA) sequence conservation, as well as HA glycosylation site, NA resistance site and key amino acid sites of 6 internal gene-encoded proteins were analyzed, meanwhile, the receptor binding ability of the two strains was determined as well. The results suggested that the HA protein cleavage site of CK93 was PEIPKGR↓GLF, which indicated a low pathogenicity of CK93, whereas CK207 was mutated to PKPKRTAR↓GLF, which indicated a high pathogenicity of CK207. At the same time, the 226 amino acid sequence of HA in CK93 was Leucine (226L), while its counterpart in CK207 was Glutamine (226Q). However, the receptor binding ability results suggested that two isolates can be bound to both α-2,3 sialic acid receptor and α-2,6 sialic acid receptor, it is indicated that the Q226L is not a decisive factor affecting receptor binding characteristics. In light of the above information, it is suggested that precaution and control to the mutation of H7N9 subtype avian influenza should be enhanced in order to lower any risk of epidemic owing to its mutation.

Key words: H7N9 subtype avian influenza virus, molecular characterization analysis, receptor-binding specificities

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