SUMMARYThe electrophoretic mobilities of the two genome segments and the structural polypeptides of the chicken strain Cu-1 (serotype I) and the turkey isolate 23/82 (serotype II) of infectious bursal disease virus were compared. There is a close antigenic relationship between the smaller of the two major structural proteins (32K) of both strains. Neutralizing monoclonal antibodies are induced by the larger protein (40K in Cu-1) which differentiates between the two serotypes. The 40K structural protein also has epitopes which do not induce neutralizing antibodies and which are common to both strains. There is evidence that the antigenic region responsible for the production of neutralizing antibodies is highly conformation-dependent. Passively administered neutralizing antibodies directed against the 40K structural polypeptide of Cu-1 confer protective immunity to susceptible chickens, whereas antibodies directed against the 32K structural protein do not have any protective effect.
INTRODUCTIONThe basic structure of the infectious bursal disease virus (IBDV), the aetiological agent of a disease of chickens which results in the destruction of the bursa of Fabricius, has been elucidated (Nick et al., 1976; M/iller et al., 1979) and has been shown to exhibit the structural characteristics of the Birnaviridae (Dobos et al., 1979;Brown, 1986). During the past few years isolates of IBDV from turkeys have been reported to be essentially identical to the chicken strains, but the turkey isolates were not pathogenic and could be distinguished by neutralization (McNulty et al., 1979;Jackwood et al., 1982); a second serotype was therefore established (McFerran et al., 1980). In order to localize the antigenic determinants on the structural proteins of IBDV which are responsible for the induction of neutralizing antibodies, a more detailed comparative analysis of the two types of viruses was necessary. Attempts were therefore made to obtain more precise information about the size of the two genomic segments ofdsRNA and the structural proteins of the turkey strain in relation to the known elements of the chicken virus. The antigenic sites which both types of viruses have in common and those which permit their distinction were traced with monoclonal antibodies. The need for a more precise analysis of the antigenic structure of IBDV was underlined by the attempts of other authors to describe antigenic regions which would lend themselves to the production of a vaccine in Escherichia coli or by peptide synthesis (Fahey et al., 1985a,b;Azad et al., 1986;Hudson et al., 1986).