Citation: TANG Qing, Lillian A Orciari Charles E.Rupprechti, ZHAO Xiu-Qin, LI Zhi-Gang, YANG Wei-Song. Sequencing and position analysis of the glycoprotein gene of four Chinese rabies viruses .VIROLOGICA SINICA, 2000, 15(1) : 22.

Sequencing and position analysis of the glycoprotein gene of four Chinese rabies viruses

  • Available online: 05 March 2000
  • The glycoprotein gene of human rabies vaccine strain (aG), one attenuated fixed strain (CTN 181) and two street viruses were sequenced and the amino acid sequences were deduced. The result shows that two street strains have two differences in nucleotide sequences and one in amino acid sequences, the nucleotide homology was higher compared with CTN (85.9%) than with aG (81.9%). Phylogenetic tree divided the street strains and the laboratory strains into two branches. High amino acid sequence similarity was present between the segments of the viral GP which may function as a recognition site for AchR and the receptor binding region of the neurotoxins; CTN strain had Q substitution at position 333 and the other virulent strains preserved 333 Arg. In all strains 319 glycosylation was existed, glycosylation on 37 is also relatively conserved. The amino acid constitution of antigenic site Ⅱ is identical in all compared strains, but on site Ⅲ some attenuated strains have amino acid substitution on position 333 and

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    Sequencing and position analysis of the glycoprotein gene of four Chinese rabies viruses

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    Abstract: The glycoprotein gene of human rabies vaccine strain (aG), one attenuated fixed strain (CTN 181) and two street viruses were sequenced and the amino acid sequences were deduced. The result shows that two street strains have two differences in nucleotide sequences and one in amino acid sequences, the nucleotide homology was higher compared with CTN (85.9%) than with aG (81.9%). Phylogenetic tree divided the street strains and the laboratory strains into two branches. High amino acid sequence similarity was present between the segments of the viral GP which may function as a recognition site for AchR and the receptor binding region of the neurotoxins; CTN strain had Q substitution at position 333 and the other virulent strains preserved 333 Arg. In all strains 319 glycosylation was existed, glycosylation on 37 is also relatively conserved. The amino acid constitution of antigenic site Ⅱ is identical in all compared strains, but on site Ⅲ some attenuated strains have amino acid substitution on position 333 and

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