一种与乙型肝炎表面抗原免疫显性区域紧密相互作用的噬菌体展示环肽。

A phage-displayed cyclic peptide that interacts tightly with the immunodominant region of hepatitis B surface antigen.

作者信息

Tan Wen Siang, Tan Geok Hun, Yusoff Khatijah, Seow Heng Fong

机构信息

Department of Microbiology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400 UPM Serdang, Selangor, Malaysia.

出版信息

J Clin Virol. 2005 Sep;34(1):35-41. doi: 10.1016/j.jcv.2005.01.007.

DOI:10.1016/j.jcv.2005.01.007

PMID:16087122

Abstract

The surface antigen (HBsAg) of hepatitis B virus (HBV) is highly conformational and generally evokes protective humoral immune response in human. A disulfide constrained random heptapeptide library displayed on the coat protein III of filamentous bacteriophage M13 was employed to select specific ligands that interact with HBsAg subtype ad. Fusion phages carrying the amino acid sequence ETGAKPH and other related sequences were isolated. The binding site of peptide ETGAKPH was located on the immunodominant region of HBsAg. An equilibrium binding assay in solution showed that the phage binds tightly to HBsAg with a relative dissociation constant (KDrel) of 2.9+/-0.9 nM. The phage bearing this peptide has the potential to be used as a diagnostic reagent and two assays for detecting HBsAg in blood samples are described.

摘要

乙型肝炎病毒（HBV）的表面抗原（HBsAg）具有高度的构象，通常会在人体中引发保护性体液免疫反应。利用展示在丝状噬菌体M13外壳蛋白III上的二硫键约束随机七肽库来筛选与HBsAg ad亚型相互作用的特异性配体。分离出携带氨基酸序列ETGAKPH及其他相关序列的融合噬菌体。肽ETGAKPH的结合位点位于HBsAg的免疫显性区域。溶液中的平衡结合试验表明，该噬菌体与HBsAg紧密结合，相对解离常数（KDrel）为2.9±0.9 nM。携带此肽的噬菌体有潜力用作诊断试剂，并描述了两种检测血样中HBsAg的检测方法。