ArticleVirology journal2010
Identification of a novel linear B-cell epitope in the UL26 and UL26.5 proteins of Duck Enteritis Virus.
Article in Virology journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 9 citations in OpenAlex.
- First complete genome characterization of duck plague virus from India.Virusdisease · 2021Article
- Analyzing and identifying novel B cell epitopes within Toxoplasma gondii GRA4.Parasites & vectors · 2014Article
- Adaptation and attenuation of duck Tembusu virus strain Du/CH/LSD/110128 following serial passage in chicken embryos.Clinical and vaccine immunology : CVI · 2014Article
- Evaluation of a recombinant multiepitope peptide for serodiagnosis of Toxoplasma gondii infection.Clinical and vaccine immunology : CVI · 2012Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe Unique Long 26 (UL26) and UL26.5 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 UL26.5, 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 UL26.5 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.
resultsA 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 UL26.5 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.
conclusionA mAb, 1C8, was generated against DEV UL26c and the epitope-defined minimal sequence obtained using mAb 1C8 was ⁵²⁰IYYPGE⁵²⁵. The mAb and the identified epitope may be useful for further study of the design of diagnostic reagents for DEV.
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