Prediction of the secondary structure and B cell epitopes of human metapneumovirus attachment protein
Objective To predict the secondary structure and B cell epitopes of human metapneumovirus attachment(G) protein.Methods The secondary structure and transmembrane domain were predicted by SOPMA and HMMTOP respectively. Hydrophilicity profile, surface probability and antigenicity index predicted by methods of Kyte-Doolittle, Emini and Jameson-Wolf were combined and the possible B cell epitopes of G protein were predicted.Results The flexible regions were the main structure type, locating at the N-terminal No.27-31, 38-39, 56-77, 81-124, 131-146, 151-167, 180-188, 193-212 regions. There were α-helix regions at the N-terminal No.5-26, 40-46, 125-130, 168-175, 213-218. And the N-terminal No.1-4, 32-37, 47-55, 78-80, 147-150, 176-179, 189-192 were the β-sheet regions. The N-terminal No.32-51 was the transmembrane domain. B cell epitopes were probably located at or adjacent the N-terminal No.55-77, 80-104, 111-126, 130-167, 178-210 regions, and the former three fragments were the predominant epitopes.Conclusion Prediction of the secondary structure and B cell epitopes of G protein lay the basis for studies of the characteristics of the protein, development of epitope-based vaccine and the monoclonal antibody against G protein.