Secondary structure and prediction of B cell epitope of F protein in respiratory syncytial virus
YI Gao
PAN Jiayu
LIN Chunyi
LIU Zhaoyu
Abstract：Objective To analyze the secondary structure and predict its B cell epitope of F protein in respiratory syncytial virus ( RSV) .Methods We analyzed the secondary structure of RSV F protein and obtained the sequence and location about the signal peptide in RSV F protein.Based on the homology modeling method, we predicted the potential conformational B epitopes and linear B epitopes in RSV F protein.Results Among the 574 amino acids of RSV F protein, the major amino acids were serine (10.45%), leucine (10.28), asparagine (8.71%) and threonine (8.71%).There might be 7 protein binding sites, 6 helical structure generation regions and 2β-plated sheets in F protein.The sites 1-25 of N-terminus in F protein were signaling peptides.The head of the F protein was mainly composed byβ-plated sheets, ran-dom coils and turns, while the tail was mainly composed by 2 long α-helixes.Eight linear B epitopes and four conforma-tional B epitopes were predicted in F protein.Conclusions Serine and leucine occupy the maximum ratio of amino acids encoding F protein.There might be seven protein binding sites, six helical structure generation regions, two majorβ-plated sheets in F protein, and RSV F protein may contain four conformational B epitopes and eight linear B epitopes.
Keywords：respiratory syncytial virusF proteinsecondary structure of proteinB cell epitope
Publication Date：2016-01-01
Online Publishing Date：2025-08-15(First online date of this platform, not the publication date of the document)
Pages：4( 20-23 )