Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
6142761 | Virus Research | 2013 | 5 Pages |
SigmaC (ÏC) protein, which mediates virus attachment to target cells, is the most variable proteins of avian reovirus (ARV). It is responsible for inducing protective antibody immune responses in animals. To understand the antigenic determinants of ÏC protein, a set of partially overlapping and consecutive peptides spanning ÏC were expressed and then screened with the monoclonal antibody (mAb) 2B5 directed against ÏC. The mAb 2B5 recognized peptides with the ÏC motif 45ELLHRSISDISTTV58. Further identification of the displayed B-cell epitope was conducted with a set of truncated peptides expressed as GST fusion proteins. The Western blot and ELISA results indicated that 45ELLHRSISDI54 was the minimal determinant of the linear B-cell epitope. Using sequences analysis, we found that this epitope was not a common motif shared among the other members of the ARV and DRV groups. Furthermore, cross reactivity analysis showed that the associated coding motif of other ARV and DRV groups was not recognized by 2B5. These data suggested that 45ELLHRSISDI54 was a type-specific linear B-cell epitope of avian reovirus. The results in this study may have potential applications in the development of diagnostic techniques and epitope-based marker vaccines against ARV, which is prevalent in China.