Liang X P, Babiuk L A, Zamb T J
Veterinary Infectious Disease Organization, University of Saskatchewan, Saskatoon, Canada.
J Virol. 1991 Oct;65(10):5553-7. doi: 10.1128/JVI.65.10.5553-5557.1991.
The gIII glycoproteins of bovine herpesvirus 1 (BHV-1) and of pseudorabies virus (PRV) are structurally homologous. Both proteins also play preeminent roles in mediating virus attachment to permissive cells. To directly compare the functional relation between these glycoproteins, we constructed a recombinant BHV-1 in which the BHV-1 gIII coding sequence was replaced by the PRV gene homolog. The resultant recombinant virus efficiently expressed PRV gIII and then incorporated it into its envelope. The levels of PRV gIII expression and incorporation were equivalent to those achieved by the wild-type virus for BHV-1 gIII. The recombinant virus was fully susceptible to neutralization by anti-PRV gIII neutralizing antibody. In addition, the virus attachment and penetration functions, as well as the virus replication efficiency, which were lost by deleting the BHV-1 gIII gene, were restored by expressing the PRV gIII homolog in its place. These results demonstrated that PRV gIII and BHV-1 gIII share complementary functions.
牛疱疹病毒1型（BHV-1）和伪狂犬病病毒（PRV）的gIII糖蛋白在结构上具有同源性。这两种蛋白在介导病毒与易感细胞的附着过程中也都发挥着重要作用。为了直接比较这些糖蛋白之间的功能关系，我们构建了一种重组BHV-1，其中BHV-1的gIII编码序列被PRV的同源基因所取代。所得的重组病毒高效表达PRV gIII，并将其整合到病毒包膜中。PRV gIII的表达水平和整合水平与野生型病毒表达BHV-1 gIII时所达到的水平相当。该重组病毒完全可被抗PRV gIII中和抗体中和。此外，通过在缺失BHV-1 gIII基因的位置表达PRV gIII同源物，恢复了因缺失BHV-1 gIII基因而丧失的病毒附着和穿透功能以及病毒复制效率。这些结果表明PRV gIII和BHV-1 gIII具有互补功能。
