@article{mbs:/content/journal/jgv/10.1099/0022-1317-64-3-693, author = "Coulon, P. and Rollin, P. E. and Flamand, A.", title = "Molecular Basis of Rabies Virus Virulence. II. Identification of a Site on the CVS Glycoprotein Associated with Virulence", journal= "Journal of General Virology", year = "1983", volume = "64", number = "3", pages = "693-696", doi = "https://doi.org/10.1099/0022-1317-64-3-693", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-64-3-693", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", keywords = "rabies virus", keywords = "monoclonal antibody", keywords = "avirulent mutants", keywords = "glycoprotein", abstract = "SUMMARY Nine anti-G monoclonal antibodies were used to select mutants of the CVS strain of rabies virus resistant to neutralization. Seven mutants were avirulent in adult mice and two others exhibited an attenuated pathogenicity. Both categories were resistant to monoclonal antibodies 194-2 and 248-8. Virulence appears to be associated with a particular configuration of a region of the glycoprotein which is located at the intersection of the epitopes recognized by these two monoclonal antibodies. Our results confirm the role played by the glycoprotein in the neurovirulence of rabies virus.", }