A conformational epitope mapped in the bovine herpesvirus type 1 envelope glycoprotein B by phage display and the HSV-1 3D structure

作者：Almeida Greyciele R; Goulart Luiz Ricardo; Cunha Junior Jair P; Bataus Luiz A M; Japolla Greice; Brito Wilia M E D; Campos Ivan T N; Ribeiro Cristina; Souza Guilherme R L^*

来源：Research in Veterinary Science, 2015, 101: 34-37.

DOI：10.1016/j.rvsc.2015.05.021

• BoHV-1
• Glycoprotein B
• Epitope mapping
• Discontinuous epitope
• Structural homology

The selected dodecapeptide (1)DRALYGPTVIDH(12) from a phage-displayed peptide library and the crystal structure of the envelope glycoprotein B (Env gB) from Herpes Simplex Virus type 1 (HSV-1) led us to the identification of a new discontinuous epitope on the Bovine herpesvirus type 1 (BoHV-1) Env gB. In silico analysis revealed a short BoHV-1 gB motif ((YKRD341)-Y-338) within a epitope region, with a high similarity to the motifs shared by the dodecapeptide N-terminal region ((5)YxARD(1)) and HSV-1 Env gB ((326)YARD(329)), in which the (328)Arg residue is described to be a neutralizing antibody target. Besides the characterization of an antibody-binding site of the BoHV-1 Env gB, we have demonstrated that the phage-fused peptide has the potential to be used as a reagent for virus diagnosis by phage-ELISA assay, which discriminated B0HV-1 infected serum samples from negative ones.

• 出版日期2015-8