Identification of a conserved conformational epitope in the VP2 protein of foot-and-mouth disease virus
文献类型： 外文期刊
作者： Liu, Wenming 1 ; Yang, Baolin 1 ; Wang, Mingxia 1 ; Liang, Weifeng 1 ; Wang, Haiwei 1 ; Yang, Decheng 1 ; Ma, Wenge; Z 1 ;
作者机构： 1.Chinese Acad Agr Sci, Harbin Vet Res Inst, Div Livestock Infect Dis, State Key Lab Vet Biotechnol, 678 Haping Rd, Harbin 150069, Peoples R China
2.Ch
期刊名称：ARCHIVES OF VIROLOGY （ 影响因子：2.574； 五年影响因子：2.466 ）
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收录情况： SCI
摘要： Foot-and-mouth disease (FMD), caused by foot-and-mouth disease virus (FMDV), is a highly contagious infectious disease that affects domestic and wild cloven-hoofed animals worldwide. VP2 is a structural protein of FMDV. In this study, a potent FMDV serotype-independent monoclonal antibody (MAb) 3D9 was generated. Screening of a phage-displayed random 12-peptide library revealed that MAb 3D9 bound to phages displaying a consensus motif GVYxxAYxW that is highly homologous to the (89)GVYxxxxxxxAYxxxxW(105) motif in the FMDV VP2 protein. Importantly, this conformational epitope was highly conserved among all seven serotypes of FMDV analyzed in sequence alignments. To further verify the authentic epitope recognized by MAb 3D9, a FMDV O/YS/CHA/05 mutant virus V90A was generated using a reverse genetics system. The results revealed that Val(90) was an important residue for MAb 3D9 binding within this conformational epitope. Thus, we finely mapped a conserved conformational epitope onto the FMDV VP2 protein. These results could be applied in the development of epitope-based vaccines and suitable MAb-based diagnostic methods for various FMDV serotype-independent tests.
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