Properties of the Glycoprotein of infectious hematopoietic necrosis virus Public Deposited

http://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/rr172081w

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  • The glycoprotein, G, of infectious hematopoietic necrosis virus, IHNV, was shown to be the viral protein which elicits and reacts with neutralizing antibodies. The G protein also confers protective immunity on immunized susceptible salmonid hosts to IHNV. The other three structural proteins of IHNV, N, Ml, and M2, do not give rise to neutralizing antibodies. Antiserum produced to the N or M2 proteins in combination with antiserum to the G protein did not enhance the neutralization of IHNV by the G protein specific antiserum. G protein purified by column chromatography was capable of blocking the neutralizing capacity of antiserum to IHNV. Together the results indicate that only the G protein of IHNV is capable of inducing a neutralizing serum antibody response. Furthermore, a vaccine to protect IHNV sensitive salmonid hosts must be based on the G protein. IHNV isolated from selected geographic locations has been grouped into five distinct biochemical types (Hsu et al., 1986). This diversity of IHNV strains was examined by immunological cross neutralization comparisons and by protection studies using a single IHNV isolate, type 1, as the source of G protein for vaccination. It was found that the G protein from Type 1 IHNV could confer protection from challenge with the four other IHNV types. The immunological comparison of ten IHNV isolates identifies a variant group. However, only a single serotype of IHNV was defined. No direct relation between biochemical type and immunological group was found. A comparison of a temperature sensitive IHNV isolate, CO2, and a nontemperature sensitive IHNV isolate, RB1, by endoglycosidase digestion of the G protein indicates carbohydrate differences are responsible for molecular weight differences in the G protein. It is proposed that temperature sensitivity and immunological differences may also be accounted for by glycosylation variations of the G protein of IHNV CO2.
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