塞姆利基森林病毒E2包膜糖蛋白中血清学定义的线性表位

Serologically defined linear epitopes in the E2 envelope glycoprotein of Semliki Forest virus.

作者信息

Ariel N, Lehrer S, Elhanaty E, Sabo T, Brodt P, Lachmi B, Katz D, Levin R, Grosfeld H, Velan B

机构信息

Department of Biochemistry, Israel Institute for Biological Research, Ness Ziona.

出版信息

Arch Virol. 1990;113(1-2):99-106. doi: 10.1007/BF01318358.

DOI:10.1007/BF01318358

PMID:1696808

Abstract

A set of 41 overlapping peptides, representing the complete sequence of SFV-E2 protein were synthesized and analyzed in the ELISA test against murine anti-SFV sera. No single peptide was recognized by all antisera. Eight peptides were found to be highly reactive with hyperimmune anti-SFV sera. Six out of the eight peptide sequences coincide with the most hydrophilic regions of SFV-E2. Out of these, four peptides (amino acid positions 16-35, 61-80, 166-185, 286-305) that contain the least number of alphavirus conserved residues were selected. This panel constitutes the minimal number of peptides necessary and sufficient for specific recognition of hyperimmune mouse anti-SFV sera.

摘要

合成了一组代表SFV-E2蛋白完整序列的41个重叠肽，并在针对鼠抗SFV血清的ELISA试验中进行分析。没有一个肽能被所有抗血清识别。发现8个肽与超免疫抗SFV血清具有高反应性。这8个肽序列中有6个与SFV-E2的最亲水区域一致。其中，选择了4个包含最少甲病毒保守残基的肽（氨基酸位置16-35、61-80、166-185、286-305）。该肽组构成了特异性识别超免疫小鼠抗SFV血清所需的最少且足够数量的肽。