Breker-Klassen M M, Yoo D, Babiuk L A
Department of Veterinary Microbiology, Western College of Veterinary Medicine, University of Saskatchewan, Saskatoon.
Can J Vet Res. 1996 Jul;60(3):228-36.
The genes for the F and HN glycoprotein of a pathogenic field isolate of bovine parainfluenza virus type 3 (BPIV3) were isolated, converted to cDNA, and sequenced using dideoxynucleotides. The resulting nucleotide sequences were converted to protein sequence and were compared to previously sequenced glycoprotein genes with amino acid differences in the glycoproteins of isolates expressing different phenotypes. The HN glycoprotein, involved in the attachment and release of the virus, and the F glycoprotein, involved in penetration and spread of the virus, have been shown to affect pathogenicity of the virus and are the immunodominant proteins of the virus. Both the F and HN proteins have been shown to be required for syncytium formation. Our results suggest that BPIV3 viruses that exhibit greater syncytium-inducing activity in vitro have greater pathogenicity in vivo. By determining which epitopes are involved in syncytium formation and comparing the sequences and enzymatic activities of different strains of virus, it may be possible to design subunit vaccines that protect against disease.
分离出牛副流感病毒3型（BPIV3）致病野毒株的F和HN糖蛋白基因，将其转化为cDNA，并使用双脱氧核苷酸进行测序。所得核苷酸序列转化为蛋白质序列，并与先前测序的糖蛋白基因进行比较，这些基因在表达不同表型的分离株的糖蛋白中存在氨基酸差异。参与病毒附着和释放的HN糖蛋白以及参与病毒穿透和传播的F糖蛋白已被证明会影响病毒的致病性，并且是病毒的免疫显性蛋白。F蛋白和HN蛋白都已被证明是形成合胞体所必需的。我们的结果表明，在体外表现出更强合胞体诱导活性的BPIV3病毒在体内具有更强的致病性。通过确定哪些表位参与合胞体形成，并比较不同病毒株的序列和酶活性，有可能设计出预防疾病的亚单位疫苗。
