|Qin, Aijian - YANGZHOU UNIVERSITY|
|Liu, Y - YANGZHOU UNIVERSITY|
|Jin, W - YANGZHOU UNIVERSITY|
Submitted to: Wei Sheng Wu Xue
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: March 1, 2002
Publication Date: December 31, 2002
Citation: Qin, A., Liu, Y., Jin, W., Lee, L.F., Fadly, A.M. 2002. Antigen analysis of envelope gene products of avian leukosis virus subgroup J. Wei Sheng Wu Xue Bao. 42:99-104. Interpretive Summary: Subgroup J avian leukosis virus (ALV-J) is an emerging economically important virus infection that can cause cancer-like disease and other production problems in meat-type chickens. This paper describes the construction of the truncated envelope gene fragments and cloning into bacteria which expressed the truncated envelope protein. Using several monoclonal antibodies against the truncated envelope protein, two regions of the protein molecule were found to be important for the binding of antigen and antibody complex. These monoclonal antibodies are unique and can detect the presence of ALV-J in commercial chickens for infection and tumor induction. This new information is significant and useful to scientists in academia and industry who are studying the epidemiology and control of this important virus infection of chickens.
Technical Abstract: Envelope glycoprotein of avian leukosis virus subgroup J (ALV-J) determines the host range of virus infection and cross-neutralization patterns. The truncated envelope genes of ALV-J were amplified by PCR and cloned into pGEX-5X-3 vector for the expression of envGST-fusion proteins. Western blot analysis showed that the products of truncated env gene expressed in E. coli reacted with G2, JE9 and I45 monoconal antibodies (Mabs) which are specific to envelope gp85 protein. The results also showed that MabG2 and JE9 recognizing epitope in gp85 was localized between amino acid 65 to155. Mab I45 recognized the epitope at amino acid 156 to 233. These results indicated that the specificity of subgroup J virus is determined by the gp85 peptide since GST-gp85 protein expressed in E. coli is not glycosylated.