Abstract
VP-2b, a major structural protein of infectious bursal disease virus (IBDV), and its precursor protein VP-2a were separated in a soluble form from the supernatant of ultracentrifuged viruses by using a monoclonal antibody specific for VP-3, the other major structural protein, to remove soluble VP-3 and remaining virus particles. The native VP-2a/2b inhibited the majority of virus-neutralizing (VN) activity in chicken anti-IBDV sera and chickens immunized with VP-2a/2b produced VN antibodies that passively protected susceptible chickens from infection. However, the separated VP2a/2b was not as immunogenic as intact virus particles. VP-2a/2b would appear to contain a conformational epitope which is destroyed by SDS and boiling and which may prove to be of critical importance in a subunit vaccine against type 1 IBDV.