Prediction of the secondary structure and B cell epitopes of human metapneumovirus attachment protein

Abstract

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.