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Production of human blood group B antigen epitope conjugated protein in Escherichia coli and utilization of the adsorption blood group B antibody

BACKGROUND: In the process of ABO-incompatible (ABOi) organ transplantation, removal of anti-A and/or B antibodies from blood plasma is a promising method to overcome hyperacute rejection and allograft loss caused by the immune response between anti-A and/or B antibodies and the A and/or B antigens...

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Autores principales: Shang, Wenjing, Zhai, Yafei, Ma, Zhongrui, Yang, Gongjin, Ding, Yan, Han, Donglei, Li, Jiang, Zhang, Houcheng, Liu, Jun, Wang, Peng George, Liu, Xian-wei, Chen, Min
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4982269/
https://www.ncbi.nlm.nih.gov/pubmed/27514820
http://dx.doi.org/10.1186/s12934-016-0538-z
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author Shang, Wenjing
Zhai, Yafei
Ma, Zhongrui
Yang, Gongjin
Ding, Yan
Han, Donglei
Li, Jiang
Zhang, Houcheng
Liu, Jun
Wang, Peng George
Liu, Xian-wei
Chen, Min
author_facet Shang, Wenjing
Zhai, Yafei
Ma, Zhongrui
Yang, Gongjin
Ding, Yan
Han, Donglei
Li, Jiang
Zhang, Houcheng
Liu, Jun
Wang, Peng George
Liu, Xian-wei
Chen, Min
author_sort Shang, Wenjing
collection PubMed
description BACKGROUND: In the process of ABO-incompatible (ABOi) organ transplantation, removal of anti-A and/or B antibodies from blood plasma is a promising method to overcome hyperacute rejection and allograft loss caused by the immune response between anti-A and/or B antibodies and the A and/or B antigens in the recipient. Although there are commercial columns to do this work, the application is still limited because of the high production cost. RESULTS: In this study, the PglB glycosylation pathway from Campylobacter jejuni was exploited to produce glycoprotein conjugated with Escherichia coli O86:B7 O-antigen, which bears the blood group B antigen epitope to absorb blood group B antibody in blood. The titers of blood group B antibody were reduced to a safe level without changing the clotting function of plasma after glycoprotein absorption of B antibodies in the plasma. CONCLUSIONS: We developed a feasible strategy for the specific adsorption/removal of blood group antibodies. This method will be useful in ABOi organ transplantation and universal blood transfusion. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12934-016-0538-z) contains supplementary material, which is available to authorized users.
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spelling pubmed-49822692016-08-13 Production of human blood group B antigen epitope conjugated protein in Escherichia coli and utilization of the adsorption blood group B antibody Shang, Wenjing Zhai, Yafei Ma, Zhongrui Yang, Gongjin Ding, Yan Han, Donglei Li, Jiang Zhang, Houcheng Liu, Jun Wang, Peng George Liu, Xian-wei Chen, Min Microb Cell Fact Research BACKGROUND: In the process of ABO-incompatible (ABOi) organ transplantation, removal of anti-A and/or B antibodies from blood plasma is a promising method to overcome hyperacute rejection and allograft loss caused by the immune response between anti-A and/or B antibodies and the A and/or B antigens in the recipient. Although there are commercial columns to do this work, the application is still limited because of the high production cost. RESULTS: In this study, the PglB glycosylation pathway from Campylobacter jejuni was exploited to produce glycoprotein conjugated with Escherichia coli O86:B7 O-antigen, which bears the blood group B antigen epitope to absorb blood group B antibody in blood. The titers of blood group B antibody were reduced to a safe level without changing the clotting function of plasma after glycoprotein absorption of B antibodies in the plasma. CONCLUSIONS: We developed a feasible strategy for the specific adsorption/removal of blood group antibodies. This method will be useful in ABOi organ transplantation and universal blood transfusion. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12934-016-0538-z) contains supplementary material, which is available to authorized users. BioMed Central 2016-08-11 /pmc/articles/PMC4982269/ /pubmed/27514820 http://dx.doi.org/10.1186/s12934-016-0538-z Text en © The Author(s) 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Research
Shang, Wenjing
Zhai, Yafei
Ma, Zhongrui
Yang, Gongjin
Ding, Yan
Han, Donglei
Li, Jiang
Zhang, Houcheng
Liu, Jun
Wang, Peng George
Liu, Xian-wei
Chen, Min
Production of human blood group B antigen epitope conjugated protein in Escherichia coli and utilization of the adsorption blood group B antibody
title Production of human blood group B antigen epitope conjugated protein in Escherichia coli and utilization of the adsorption blood group B antibody
title_full Production of human blood group B antigen epitope conjugated protein in Escherichia coli and utilization of the adsorption blood group B antibody
title_fullStr Production of human blood group B antigen epitope conjugated protein in Escherichia coli and utilization of the adsorption blood group B antibody
title_full_unstemmed Production of human blood group B antigen epitope conjugated protein in Escherichia coli and utilization of the adsorption blood group B antibody
title_short Production of human blood group B antigen epitope conjugated protein in Escherichia coli and utilization of the adsorption blood group B antibody
title_sort production of human blood group b antigen epitope conjugated protein in escherichia coli and utilization of the adsorption blood group b antibody
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4982269/
https://www.ncbi.nlm.nih.gov/pubmed/27514820
http://dx.doi.org/10.1186/s12934-016-0538-z
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