Abstract
To understand the molecular characteristics of China human rabies vaccine strains, we report the full-length genome of the aG strain and present a comprehensive analysis of this strain and almost all available lyssavirus genomes (58 strains) from GenBank (as of Jan 6, 2011). It is generally considered that the G protein plays a predominant role in determining the pathogenicity of the virus, to this end we predicted the tertiary structure of the G protein of aG strain, CTN181 strain and wild type strain HN10 based on the crystal structure of Vesicular stomatitis virus (VSV) G. The predicted RABV G structure has a similar topology to VSV G and the ectodomain can be divided into 4 distinct domains DI — DIV. By mapping the characterized mutations to this structure between China vaccine strains and their close street strains, we speculate that the G303(P-H) mutations of CTN181 and HN10 causing DII 3D change may be associated with the II attenuated virulence in both strains. Specifically, the two signature mutations (G165P and G231P) in the aG strain are withinßsheets, suggesting that both sites are of structural importance.
Keywords: Rabies virus, Lyssavirus, Genome, Glycoprotein
Footnotes
Foundation item: This work was supported by the National Department Public Benefit Research Foundation (201103032).
Contributor Information
Qing Tang, Phone: +86-10-58900895, FAX: +86-10-58900895, Email: qtang04@sina.com.
Simon Rayner, Phone: +86-27-87199895, FAX: +86-27-87199895, Email: simon.rayner.cn@gmail.com.
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