|Nazerian, Keyvan - RETIRED- ARS|
|Yoshida, Shigeto - NIPPON ZEON JAPAN|
|Yanagida, Noboro - NIPPON ZEON JAPAN|
Submitted to: International Marek's Disease Symposium Abstracts and Proceedings
Publication Type: Abstract Only
Publication Acceptance Date: September 7, 1996
Publication Date: N/A
Technical Abstract: Marek's disease virus (MDV) glycoprotein B (gB), a highly conserved immunogenic glycoprotein, plays an important role in protective immunity. When chickens were inoculated with a recombinant fowlpox virus (FPV) expressing gB, neutralizing antibodies were produced and the chickens were protected against challenge with pathogenic strains of MDV. We have shown that gB initially synthesized as a glycosylated precursor (gp100), and then proteolytically cleaved to gp60 and gp49. Several chimeric gB genes were constructed by replacing either gp60 or gp49 of the serotype-1 gB gene with the homologous region of a serotype-2 gB using a common restriction site. Similar constructs were made with serotype 1 and 3. Recombinant FPVs with chimeric gB genes were analyzed for immunoprecipitation and IFA expression. Results show the location of the neutralizing and protective epitopes to be on the gp49 moiety of the molecule.