摘要
目的：分析确定人Ｆａｓ（Ｈ－Ｆａｓ）抗原具有死亡效应的表位区域。方法：采用可及性方案、可塑性方案，结合抗原性方案、二级结构方案预测Ｈ－Ｆａｓ抗原Ｂ细胞表位。Ｆｍｏｃ固相合成法合成部分预测表位肽段并鉴定后，经固相ＥＬＩＳＡ确定是否与具有诱导细胞凋亡（ＰＣＤ）的抗人ＦａｓｍＡｂ２Ａｌ、ＤＸ２、ＣＨ－１１反应。结果：Ｈ－Ｆａｓ抗原胞外区的Ｂ细胞表位可能位于Ｎ－末端氨基酸（ＡＡ）残基５１～７８，１０２～１１０，１４５～１５７等区域内或它们附近。用Ｆｍｏｃ固相合成法合成Ｎ－末端ＡＡ残基２～１５，５０～８３肽段，毛细管电泳鉴定合成效率，ＡＡ序列分析仪检测合成序列组成正确后，经固相ＥＬＩＳＡ法检测，抗人ＦａｓｍＡｂ２Ａ１、ＤＸ２、ＣＨ－１１均不识别Ｎ－末端１００个ＡＡ内肽段。结论：Ｈ－Ｆａｓ抗原死亡表位可能界定在１００～１５７区域。
Objective: To study the death epitope of human Fas (HFas) antigen extracellular domain. Methods: B cell epitopes of HFas antigen were predicted with accessibility and flexibility schemes associated with antigenicity, secondary structures and epitope analysis scheme. HFas antigen Nterminal residues 215 and 5083, designated B14 and P34 peptides, were synthesized with peptide synthesizer and observed whether they could be recognized by antiHFas mAb 2A1, DX2 and CH11 which could induce apoptosis of Fassensitive cells. Results: B cell epitopes were likely at or adjacent to HFas antigen Nterminal residues 5178,102110 and 145157. HFas antigen Nterminal residues 1100 could not be bound to antiHFas mAb 2A1, DX2 and CH11. Conclusion: The death epitope of HFas antigen is probably localized in the Fas Nterminal residues 100157.
出处
《第三军医大学学报》
CAS
CSCD
北大核心
1999年第5期325-328,共4页
Journal of Third Military Medical University
基金
全军"九五"重点项目
