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狂犬病病毒糖蛋白信号肽序列分析 被引量:4

Analysis of Signal Peptide Sequence of Rabies Virus Glycoprotein
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摘要 为比较不同狂犬病病毒株糖蛋白信号肽序列的差异,测定了2株固定毒(CVS、3aG株)及2株街毒(SX、PB3)的糖蛋白核苷酸序列,并推导了氨基酸序列。DNAstar软件分析表明:2株街毒糖蛋白信号肽同源性为100%,2株固定毒株同源性为84.2%,街毒株与CVS、3aG的同源性分别为78.9%和73.7%;2株街毒的信号肽序列与NCBI收录的我国近年来分离的街毒株的序列完全相同;街毒株与常用疫苗株间的同源性介于68.4%~84.2%,疫苗株PV与SRV9、PV与ERA、PV与SAG同源性均为100%。对糖蛋白信号肽疏水区(-15位到-4位)的二级结构预测和疏水值计算显示,街毒株信号肽的二级结构和疏水值均与常用疫苗株和固定株存在明显差异;在N2A细胞上效价测定显示,2株街毒的效价明显低于2株固定毒。 For seeking the difference among the signal peptides of rabies virus glycoprotein,glycoprotein gene of two fixed strains(CVS,3aG strains) and two street virus(SX,PB3) were sequenced,and their deduced amino acid sequences were also mounted.Homological analysis of signal peptide of glycoprotein demonstrated that 100% was between the two street strains,and 84.2% was of the fixed strains,and 78.9% and 73.7% were among the street strain and CVS or 3aG,respectively.The signal peptides of the street strain were exactly the same as street strains by NCBI indexed from China in recent years,homology of the signal peptides of street strains and routinely used vaccine strains ranged from 68.4%—84.2%,however,100% was observed in vaccine strains of PV and SRV9,or PV and ERA,or PV and SAG.The secondary structure prediction and hydrophobic value of hydrophobic region(-15 to-4) in signal peptide of glycoprotein of street viruses revealed that folding structure and low values were significantly different from the routinely used vaccine strains and fixed strains of rabies viruses.The titer of street strain in N2A cells was significantly lower than the fixed strains.This work implied the signal peptide of glycoprotein was associated with pathogenic effects of rabies virus,and could be used to primarily evaluate the neurotropic characteristics of street rabies virus.
出处 《吉林农业大学学报》 CAS CSCD 北大核心 2013年第3期346-350,354,共6页 Journal of Jilin Agricultural University
基金 国家自然科学基金项目(31072147 31272579) 吉林省科技发展重点项目(201009540)
关键词 狂犬病病毒 糖蛋白 信号肽 街毒株 疏水区 rabies virus glycoprotein signal peptide street rabies virus hydrophobic region
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