通过噬菌体展示鉴定出的负责血红素加氧酶-1催化活性的两个表位。

Two epitopes responsible for the catalytic activity of heme oxygenase-1 identified by phage display.

作者信息

Wei Xuran, Liu Qingjun, Gao Yaping, Yang Jun, Wang Bo, Yang Guang, Zhang Shihui, Zhou Hong

机构信息

Beijing Key Laboratory of Blood Safety and Supply Technologies Beijing Institute of Transfusion Medicine China.

Institute of Basic Medical Sciences Academy of Military Medical Sciences Beijing China.

出版信息

FEBS Open Bio. 2017 Apr 3;7(5):719-726. doi: 10.1002/2211-5463.12217. eCollection 2017 May.

DOI:10.1002/2211-5463.12217

PMID:28469983

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5407895/

Abstract

Heme oxygenase-1 (HO-1) catalyzes the oxidative degradation of heme. The catalytic mechanism of the HO-1 reaction has been determined gradually by studies of its crystal structure and HO-1 mutants. However, the neutralizing epitopes responsible for HO-1 activity remain elusive. Screening of a phage display library revealed four epitopes that could interact with the polyclonal antibody prepared by immunizing rabbits with the purified HO-1 protein. Two of these four epitopes are responsible for HO-1 catalytic activity because their antibodies were able to neutralize HO-1 activity. The results of the present study shed further light on the molecular character of HO-1.

摘要

血红素加氧酶-1（HO-1）催化血红素的氧化降解。通过对其晶体结构和HO-1突变体的研究，逐渐确定了HO-1反应的催化机制。然而，负责HO-1活性的中和表位仍然难以捉摸。对噬菌体展示文库的筛选揭示了四个可与用纯化的HO-1蛋白免疫兔子制备的多克隆抗体相互作用的表位。这四个表位中的两个负责HO-1的催化活性，因为它们的抗体能够中和HO-1活性。本研究结果进一步揭示了HO-1的分子特征。