呼吸道合胞体病毒F蛋白二级结构分析及其B细胞表位预测

摘要

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.%目的：分析呼吸道合胞体病毒（RSV） F蛋白的二级结构并预测其B细胞表位。方法分析RSV F蛋白的二级结构，得出RSV F蛋白中可能出现的信号肽序列以及位置。基于同源建模的方法预测RSV F蛋白的三级结构，以三级结构为基础预测F蛋白中可能存在的构象B表位和线性B表位。结果 F蛋白的574个编码氨基酸中占主要比例的是丝氨酸（10．45％）、亮氨酸（10．28％）、天冬酰胺（8．71％）和苏氨酸（8．71％）；可能有7个蛋白结合位点、6个产生螺旋结构的区域；可能存在两个主要的β-折叠片蛋白；F蛋白N-末端第1～25区段为信号肽。 RSV F蛋白头部主要由β-折叠片、无规则卷曲和转角组成，尾部主要由两段长的α-螺旋组成。 RSV F蛋白中可能存在4个构象B表位、8个线性B表位。结论 F蛋白编码氨基酸主要为丝氨酸和亮氨酸，可能有7个蛋白结合位点、6个产生螺旋结构的区域、两个主要的β-折叠片蛋白。RSV F蛋白中可能存在4个构象B表位、8个线性B表位。