Rabies is a viral disease causing acute encephalitis in humans or animals. Rabies virus belongs to the genus Lyssavirus, family Rabdoviridea. The virus has a single, negative-stranded RNA genome encoding five structural proteins, including nucleoprotein (N), phosphoprotein (P), matrix protein (M), glycoprotein (G) and RNA dependent RNA polymerase gene (L). All of the provinces of Iran are infected with rabies. Although there is no cure for rabies, it is totally preventable by proper vaccination. Effective vaccine can be used for pre-and post-exposure prophylaxis. Glycoprotein has a main role in pathogenicity and immunogenicity thus variation in genetic sequence of this gene leads to variation in antigenic and pathogenic properties of rabies virus. Therefore, in this study, we analyzed the antigenic sites of the glycoprotein from rabies virus strains used in vaccine manufacture and compared their epitope sequences to wild type strain. We have used RT-PCR technique to determine the genetic sequence of these strains. Phylogenetic analysis showed that the wild type street virus isolate found in Iran were related to genotype 1 (classical rabies virus) and shared a high homology with the vaccine strains. Furthermore comparison of amino acid sequences of major and minor antigenic sites between the wild type and several vaccinal strains showed that the virus had a higher homology with the vaccinal strain PV that is used to manufacture vaccines in the country.