Ewasyshyn M, Bonneau A M, Usman S, Scollard N, Klein M
Connaught Centre for Biotechnology Research, Willowdale, Ontario, Canada.
J Gen Virol. 1993 Dec;74 ( Pt 12):2781-5. doi: 10.1099/0022-1317-74-12-2781.
The role of carbohydrate moieties on the immunoprotective ability of parainfluenza virus type 3 (PIV-3) haemagglutinin-neuraminidase (HN) and fusion (F) glycoproteins was tested in hamsters. HN and F proteins were purified from detergent-solubilized virus by lentil-lectin affinity chromatography and deglycosylated by treatment with endoglycosidase F (endo F). Immunization of hamsters with either 1 or 5 micrograms of mock-treated (glycosylated) affinity-purified proteins elicited strong haemagglutination inhibition and neutralizing antibody responses 4 weeks after the primary injection. In contrast, titres were significantly lower with endo F-treated (deglycosylated) proteins. However, following the booster doses with at least 5 micrograms of antigen, glycosylated and deglycosylated proteins induced comparable antibody titres. There was no significant difference in the ability of the glycosylated or deglycosylated proteins to protect either the upper or lower respiratory tracts of immunized hamsters against PIV-3 challenge. These results suggest that the carbohydrate moieties of the HN and F proteins are not necessary for eliciting a protective response in hamsters.
在仓鼠中测试了碳水化合物部分对3型副流感病毒（PIV-3）血凝素神经氨酸酶（HN）和融合（F）糖蛋白免疫保护能力的作用。通过扁豆凝集素亲和层析从去污剂溶解的病毒中纯化HN和F蛋白，并用内切糖苷酶F（内切酶F）处理使其去糖基化。用1或5微克模拟处理（糖基化）的亲和纯化蛋白免疫仓鼠，在初次注射后4周引发强烈的血凝抑制和中和抗体反应。相比之下，经内切酶F处理（去糖基化）的蛋白的滴度显著较低。然而，在用至少5微克抗原进行加强剂量后，糖基化和去糖基化蛋白诱导出相当的抗体滴度。糖基化或去糖基化蛋白在保护免疫仓鼠的上呼吸道或下呼吸道免受PIV-3攻击方面的能力没有显著差异。这些结果表明，HN和F蛋白的碳水化合物部分对于在仓鼠中引发保护性反应不是必需的。
