畜牧兽医学报 ›› 2009, Vol. 40 ›› Issue (2): 221-227.doi:

• 预防兽医 • 上一篇    下一篇

H1N2亚型猪流感病毒HA、NP、NA、M和NS基因的克隆与序列分析

蒙雪琼1,陈义祥2*,刘棋2,郑敏2,施开创2,胡杰2   

  1. 1. 广西大学动物科学技术学院,南宁 530005;2. 广西动物疫病预防控制中心,南宁 530001
  • 收稿日期:1900-01-01 修回日期:1900-01-01 出版日期:2009-02-24 发布日期:2009-02-24
  • 通讯作者: 陈义祥

Cloning and Sequence Analysis of the HA,NP,NA,M and NS Genes of H1N2 Swine Influenza Viruses

MENG Xue-qiong1,CHEN Yi-xiang2*,LIU Qi2,ZHENG Min2,SHI Kai-chuang2, HU Jie2   

  1. 1. College of Animal Science and Technology, Guangxi University, Nanning 530005,China;2. Guangxi Center for Animal Disease Control and Prevention, Nanning 530001, China
  • Received:1900-01-01 Revised:1900-01-01 Online:2009-02-24 Published:2009-02-24

摘要: 对3株H1N2亚型猪流感病毒(SIV):Sw/GX/17/05、Sw/HN/1/05和Sw/GX/13/06的血凝素(HA)、核蛋白(NP)、神经氨酸酶(NA)、基质蛋白(M)和非结构蛋白(NS)基因进行克隆和序列分析。结果显示:3株分离毒株HA、NP、NA、M和NS基因之间核苷酸同源性分别为91.3%~98.0%、98.4%~98.8%、97.4%~98.3%、98.8%~99.8%和98.1%~98.4%。遗传进化分析显示:分离毒株与美国分离的三源基因重排H1N2 SIV具有较近的亲缘关系;在HA、NP、M和NS基因进化树中,3株分离毒株均位于古典H1N1亚型SIV群,在NA基因进化树中,3株分离毒株则位于人流感病毒群。HA和NA基因推导氨基酸序列分别与代表毒株古典H1N1 SIV A/swine/Maryland/23239/1991(H1N1)和人H3N2流感病毒A/Buenos Aires/4459/96(H3N2)比较分析显示:HA(95.4%~96.1%)和NA(96.6%~97.2%)具有较高的氨基酸同源性;糖基化位点、抗原位点和受体结合位点(HA)处氨基酸存在一定的差异,这些氨基酸差异对病毒生物学特性的影响有待于进一步研究。

Abstract: In this study,the HA, NP, NA, M and NS genes of three isolates of H1N2 swine influenza viruses (SIV) were cloned and sequenced. Sequence comparisons revealed that three isolates share a higher degree of similarity. Genetic analysis demonstrated that three isolates were closely related to the United States triple reassortant H1N2 SIV isolate. In the HA, NP, M and NS genes phylogenetic trees, three isolates clustered with classical H1N1 SIV. While in the NA gene tree, isolates clustered with human influenza viruses. Comparisons of deduced amino acid sequences of HA and NA of the 3 isolates with the representative viruses A/swine/Maryland/23239/1991 (H1N1) and A/Buenos Aires/4459/96 (H3N2) revealed that they shared 954%961% (HA) and 966%972% (NA) amino acid similarities, respectively. Amino acid substitutions were detected at previously defined glycosylation sites, antigenic sites and receptor binding sites of the HA or NA proteins. The effects of isolates owing to these amino acid substitutions on biological characterization are unknown.