Next Article in Journal
From ELF to Compressibility in Solids
Previous Article in Journal
Chemical Conversion Pathways and Kinetic Modeling for the OH-Initiated Reaction of Triclosan in Gas-Phase
Article Menu
Issue 4 (April) cover image

Export Article

Open AccessCommunication
Int. J. Mol. Sci. 2015, 16(4), 8142-8150; doi:10.3390/ijms16048142

Characterization of the Recognition Specificity of BH2, a Monoclonal Antibody Prepared against the HLA-B27 Heavy Chain

1
Department of Life Science and Institute of Molecular Biology, National Chung Cheng University, Chia-Yi 621, Taiwan
2
Section of Allergy, Immunology and Rheumatology, Department of Medicine, Buddhist DaLin Tzu-Chi Hospital, Chia-Yi 622, Taiwan
3
School of Medicine, Tzu-Chi University, Hualien 970, Taiwan
4
Department of Nutrition and Health Science, Fooyin University, Kaohsiung 831, Taiwan
5
Department of Chemical Engineering, National Chung Cheng University, Chia-Yi 621, Taiwan
These authors contributed equally to this work.
*
Authors to whom correspondence should be addressed.
Academic Editor: Denis Girard
Received: 30 January 2015 / Revised: 18 March 2015 / Accepted: 3 April 2015 / Published: 13 April 2015
(This article belongs to the Section Biochemistry, Molecular and Cellular Biology)
View Full-Text   |   Download PDF [1934 KB, uploaded 13 April 2015]   |  

Abstract

BH2, a monoclonal antibody prepared against the denatured human leukocytic antigen-B27 heavy chain (HLA-B27 HC), can immunoprecipitate the misfolded HLA-B27 HC complexed with Bip in the endoplasmic reticulum and recognize the homodimerized HLA-B27 HC that is often observed on the cell membrane of patients suffered from ankylosing spondylitis (AS). However, the recognition specificity of BH2 toward the other molecules of HLA-B type and toward the different types of HLA molecules remained uncharacterized. In this study, we carried out the HLA-typing by using the Luminex Technology to characterize the recognition specificity of BH2 and analyzed the binding domain of HLA-B27 HC by BH2. Our results indicated that BH2 preferably binds to molecules of HLA-B and -C rather than HLA-A and the binding site is located within the α2 domain of HLA-B27 HC. View Full-Text
Keywords: HLA-B27; ankylosing spondylitis; monoclonal antibody; HLA-typing HLA-B27; ankylosing spondylitis; monoclonal antibody; HLA-typing
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Yu, H.-C.; Huang, K.-Y.; Lu, M.-C.; Huang, H.-L.; Liu, W.-T.; Lee, W.-C.; Liu, S.-Q.; Huang, H.-B.; Lai, N.-S. Characterization of the Recognition Specificity of BH2, a Monoclonal Antibody Prepared against the HLA-B27 Heavy Chain. Int. J. Mol. Sci. 2015, 16, 8142-8150.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top