tailieunhanh - Báo cáo y học: " Identification of a novel linear B-cell epitope in the UL26 and UL26.5 proteins of Duck Enteritis Virus"

Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành y học dành cho các bạn tham khảo đề tài: Identification of a novel linear B-cell epitope in the UL26 and proteins of Duck Enteritis Virus | Liu et al. Virology Journal 2010 7 223 http content 7 1 223 VIROLOGY JOURNAL RESEARCH Open Access Identification of a novel linear B-cell epitope in the UL26 and proteins of Duck Enteritis Virus Xiaoli Liu Zongxi Han Yuhao Shao Dan Yu Huixin Li Yu Wang Xiangang Kong Shengwang Liu Abstract Background The Unique Long 26 UL26 and proteins of herpes simplex virus are known to function during the assembly of the viruses. However for duck enteritis virus DEV which is an unassigned member of the family Herpesviridae little information is available about the function of the two proteins. In this study the C-terminus of DEV UL26 protein designated UL26c which contains the whole of was expressed and the recombinant UL26c protein was used to immunize BALB c mice to generate monoclonal antibodies mAb . The mAb 1C8 was generated against DEV UL26 and proteins and used subsequently to map the epitope in this region. Both the mAb and its defined epitope will provide potential tools for further study of DEV. Results A mAb designated 1C8 was generated against the DEV UL26c protein and a series of 17 partially overlapping fragments that spanned the DEV UL26c were expressed with GST tags. These peptides were subjected to enzyme-linked immunosorbent assay ELISA and western blotting analysis using mAb 1C8 to identify the epitope. A linear motif 520IYYPGE525 which was located at the C-terminus of the DEV UL26 and proteins was identified by mAb 1C8. The result of the ELISA showed that this epitope could be recognized by DEV-positive serum from mice. The 520IYYPGE525 motif was the minimal requirement for reactivity as demonstrated by analysis of the reactivity of 1C8 with several truncated peptides derived from the motif. Alignment and comparison of the 1C8-defined epitope sequence with those of other alphaherpesviruses indicated that the motif 521YYPGE525 in the epitope sequence was conserved among the alphaherpesviruses. Conclusion A .

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