| Literature DB >> 24076298 |
Chun-hong Yin1, Li-ting Qin, Mei-yu Sun, Yu-long Gao, Xiao-le Qi, Hong-lei Gao, Yong-qiang Wang, Li-li Jang, Xiao-mei Wang.
Abstract
SigmaC (σC) 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 σC protein, a set of partially overlapping and consecutive peptides spanning σC were expressed and then screened with the monoclonal antibody (mAb) 2B5 directed against σC. The mAb 2B5 recognized peptides with the σC motif (45)ELLHRSISDISTTV(58). 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 (45)ELLHRSISDI(54) 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 (45)ELLHRSISDI(54) 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.Entities:
Keywords: Avian reovirus; Cross reactivity analysis; Linear B-cell epitope; SigmaC protein
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Year: 2013 PMID: 24076298 DOI: 10.1016/j.virusres.2013.09.028
Source DB: PubMed Journal: Virus Res ISSN: 0168-1702 Impact factor: 3.303