Lorenzen N, Olesen N J, Jørgensen P E
National Veterinary Laboratory, Arhus N, Denmark.
J Gen Virol. 1990 Mar;71 ( Pt 3):561-7. doi: 10.1099/0022-1317-71-3-561.
Egtved virus, the rhabdovirus causing viral haemorrhagic septicaemia in rainbow trout, was analysed at the antigen level with a future subunit vaccine in mind. Three monoclonal antibodies to the viral G protein were characterized with respect to neutralizing activity at the cell culture level, as well as their ability to protect rainbow trout fingerlings against virus infection following passive immunization. Two antibodies showed strong protective activity in fish. Only one of these antibodies was able to neutralize viral infectivity in vitro. Reduction of disulphide bonds in the G protein abolished reactivity of this antibody in immunoblotting, whereas antigen deglycosylation did not influence the binding ability of any of the antibodies. These data suggest that the G protein contains linear as well as non-linear, carbohydrate-free epitopes, which are involved in the protection against Egtved virus. However, an indirect influence of oligosaccharide side chains on epitope formation could not be excluded, since in situ inhibition of glycosylation prevented the binding of the protecting antibodies in immunofluorescence.
艾格特维德病毒是一种可导致虹鳟鱼病毒性出血性败血症的弹状病毒，为了研发未来的亚单位疫苗，对其进行了抗原水平分析。针对该病毒的G蛋白制备了三种单克隆抗体，并在细胞培养水平上对其中和活性进行了表征，同时还研究了它们在被动免疫后保护虹鳟鱼苗免受病毒感染的能力。两种抗体在鱼体中表现出强大的保护活性。其中只有一种抗体能够在体外中和病毒感染性。G蛋白中二硫键的还原消除了该抗体在免疫印迹中的反应性，而抗原去糖基化并不影响任何一种抗体的结合能力。这些数据表明，G蛋白包含线性和非线性的、无碳水化合物的表位，这些表位参与了对艾格特维德病毒的保护。然而，由于糖基化的原位抑制阻止了保护抗体在免疫荧光中的结合，因此不能排除寡糖侧链对表位形成的间接影响。
