The genome of bovine ephemeral fever rhabdovirus contains two related glycoprotein genes

Genome organization and transcription strategy in the complex GNS-L intergenic region of bovine ephemeral fever rhabdovirus.

“…The Beijing-1 strain of BEFV was isolated from the blood of an infected cow at Beijing, China in 1976 (Bai et al, 1987). The viruses were grown in BHK-21 cells at 37 mC in RPMI 1640 or BME medium supplemented with 14 mM HEPES, 10 % foetal calf serum, 100 U\ml penicillin and 100 µg\ml streptomycin as described previously (Walker et al, 1991(Walker et al, , 1992.…”

“…Amino acid sequence analysis of the BEFV nucleoprotein (N) has indicated a close relationship to that of ARV and similarity to other animal rhabdoviruses with higher overall homology to vesiculoviruses than to lyssaviruses Wang et al, 1995). However, the BEFV and ARV genomes are more complex than other rhabdoviruses as each contains two consecutive glycoprotein genes (Walker et al, 1992 ;Wang & Walker, 1993). The first encodes the virion envelope glycoprotein (G) which contains type-specific and neutralizing antigenic sites (Cybinski et al, 1990) and protects cattle against experimental infection (Uren et al, 1994 ;Hertig et al, 1996).…”

“…The first encodes the virion envelope glycoprotein (G) which contains type-specific and neutralizing antigenic sites (Cybinski et al, 1990) and protects cattle against experimental infection (Uren et al, 1994 ;Hertig et al, 1996). The second gene also encodes a class 1 transmembrane glycoprotein (G NS ) which has not been detected in virions and does not induce a protective or neutralizing immune response (Walker et al, 1991(Walker et al, , 1992Hertig et al, 1996). The G and G NS proteins are related to each other both in structure and in amino acid sequence and to virion G proteins of other rhabdoviruses and appear to have arisen by gene duplication (Wang & Walker, 1993).…”

Bovine Ephemeral Fever in Taiwan

“…Each virus was purified by 3 rounds of limited dilution, expanded, and cleared by centrifugation at 2,000 ϫ g for 25 min at 4 C. The supernatant containing viral particles was used for RNA extraction by mixing 0.25 ml of virus suspension with 0.75 ml of Trizol . b Half of the pelleted RNA was used for one reverse transcription reaction, 26 23 where GF1 were 5Ј-ATGTTCA-AGGTCCTCATAATTACC-3Ј (1-24) and GR1 were 5Ј-TAATGATCAAAGAACCTATCATCAC-3Ј (1,847-1,871). The reaction mixture was denatured at 94 C for 4 minutes, followed by 30 cycles of amplification at 94 C for 45 seconds, 52 C for 60 seconds, and 72 C for 90 seconds, with a final extension at 72 C for 10 minutes.…”

Deduced structural model for animal rhabdovirus glycoproteins.

“…Although G proteins of rhabdoviruses from different genera share a very low level of amino acid sequence identity, alignment of the sequences reveals remarkable conservation of cysteine residues, glycosylation sites and the major antigenic domains. Of particular significance is the alignment of 12 highly conserved cysteine residues and elements of a common discontinuous antigenic site comprising widely separated regions of the polypeptide chain (Walker et al, 1992 ;Huang et al, 1996 ;Kongsuwan et al, 1998). The extent of these similarities suggests that, despite the wide differences in host range and tissue tropism, the core elements of animal rhabdovirus G protein structure are preserved.…”