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

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...

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Detalles Bibliográficos
Autores principales: Wei, Xuran, Liu, Qingjun, Gao, Yaping, Yang, Jun, Wang, Bo, Yang, Guang, Zhang, Shihui, Zhou, Hong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2017
Materias:
Research Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5407895/
https://www.ncbi.nlm.nih.gov/pubmed/28469983
http://dx.doi.org/10.1002/2211-5463.12217
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author Wei, Xuran
Liu, Qingjun
Gao, Yaping
Yang, Jun
Wang, Bo
Yang, Guang
Zhang, Shihui
Zhou, Hong
author_facet Wei, Xuran
Liu, Qingjun
Gao, Yaping
Yang, Jun
Wang, Bo
Yang, Guang
Zhang, Shihui
Zhou, Hong
author_sort Wei, Xuran
collection PubMed
description 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.
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spelling pubmed-54078952017-05-03 Two epitopes responsible for the catalytic activity of heme oxygenase‐1 identified by phage display Wei, Xuran Liu, Qingjun Gao, Yaping Yang, Jun Wang, Bo Yang, Guang Zhang, Shihui Zhou, Hong FEBS Open Bio Research Articles 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. John Wiley and Sons Inc. 2017-04-03 /pmc/articles/PMC5407895/ /pubmed/28469983 http://dx.doi.org/10.1002/2211-5463.12217 Text en © 2017 The Authors. Published by FEBS Press and John Wiley & Sons Ltd. This is an open access article under the terms of the Creative Commons Attribution (http://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Articles
Wei, Xuran
Liu, Qingjun
Gao, Yaping
Yang, Jun
Wang, Bo
Yang, Guang
Zhang, Shihui
Zhou, Hong
Two epitopes responsible for the catalytic activity of heme oxygenase‐1 identified by phage display
title Two epitopes responsible for the catalytic activity of heme oxygenase‐1 identified by phage display
title_full Two epitopes responsible for the catalytic activity of heme oxygenase‐1 identified by phage display
title_fullStr Two epitopes responsible for the catalytic activity of heme oxygenase‐1 identified by phage display
title_full_unstemmed Two epitopes responsible for the catalytic activity of heme oxygenase‐1 identified by phage display
title_short Two epitopes responsible for the catalytic activity of heme oxygenase‐1 identified by phage display
title_sort two epitopes responsible for the catalytic activity of heme oxygenase‐1 identified by phage display
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5407895/
https://www.ncbi.nlm.nih.gov/pubmed/28469983
http://dx.doi.org/10.1002/2211-5463.12217
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