Cargando…
Development of a high yield expression and purification system for Domain I of Beta-2-glycoprotein I for the treatment of APS
BACKGROUND: In this paper we describe a novel method to achieve high yield bacterial expression of a small protein domain with considerable therapeutic potential; Domain I of Beta-2-glycoprotein I (β2GPI). β2GPI is intrinsic to the pathological progression of the Antiphospholipid Syndrome (APS). Pat...
Autores principales: | , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4650279/ https://www.ncbi.nlm.nih.gov/pubmed/26576675 http://dx.doi.org/10.1186/s12896-015-0222-0 |
_version_ | 1782401466435108864 |
---|---|
author | McDonnell, Thomas Pericleous, Charis Laurine, Emmanuelle Tommasi, Rita Garza-Garcia, Acely Giles, Ian Ioannou, Yiannis Rahman, Anisur |
author_facet | McDonnell, Thomas Pericleous, Charis Laurine, Emmanuelle Tommasi, Rita Garza-Garcia, Acely Giles, Ian Ioannou, Yiannis Rahman, Anisur |
author_sort | McDonnell, Thomas |
collection | PubMed |
description | BACKGROUND: In this paper we describe a novel method to achieve high yield bacterial expression of a small protein domain with considerable therapeutic potential; Domain I of Beta-2-glycoprotein I (β2GPI). β2GPI is intrinsic to the pathological progression of the Antiphospholipid Syndrome (APS). Patients develop autoantibodies targeting an epitope located on the N-terminal Domain I of β2GPI rendering this domain of interest as a possible therapeutic. RESULTS: This new method of production of Domain I of β2GPI has increased the production yield by ~20 fold compared to previous methods in E.coli. This largely scalable, partially automated method produces 50–75 mg of pure, folded, active Domain I of β2GPI per litre of expression media. CONCLUSION: The application of this method may enable production of Domain I on sufficient scale to allow its use as a therapeutic. |
format | Online Article Text |
id | pubmed-4650279 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-46502792015-11-19 Development of a high yield expression and purification system for Domain I of Beta-2-glycoprotein I for the treatment of APS McDonnell, Thomas Pericleous, Charis Laurine, Emmanuelle Tommasi, Rita Garza-Garcia, Acely Giles, Ian Ioannou, Yiannis Rahman, Anisur BMC Biotechnol Methodology Article BACKGROUND: In this paper we describe a novel method to achieve high yield bacterial expression of a small protein domain with considerable therapeutic potential; Domain I of Beta-2-glycoprotein I (β2GPI). β2GPI is intrinsic to the pathological progression of the Antiphospholipid Syndrome (APS). Patients develop autoantibodies targeting an epitope located on the N-terminal Domain I of β2GPI rendering this domain of interest as a possible therapeutic. RESULTS: This new method of production of Domain I of β2GPI has increased the production yield by ~20 fold compared to previous methods in E.coli. This largely scalable, partially automated method produces 50–75 mg of pure, folded, active Domain I of β2GPI per litre of expression media. CONCLUSION: The application of this method may enable production of Domain I on sufficient scale to allow its use as a therapeutic. BioMed Central 2015-11-14 /pmc/articles/PMC4650279/ /pubmed/26576675 http://dx.doi.org/10.1186/s12896-015-0222-0 Text en © McDonnell et al. 2015 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 | Methodology Article McDonnell, Thomas Pericleous, Charis Laurine, Emmanuelle Tommasi, Rita Garza-Garcia, Acely Giles, Ian Ioannou, Yiannis Rahman, Anisur Development of a high yield expression and purification system for Domain I of Beta-2-glycoprotein I for the treatment of APS |
title | Development of a high yield expression and purification system for Domain I of Beta-2-glycoprotein I for the treatment of APS |
title_full | Development of a high yield expression and purification system for Domain I of Beta-2-glycoprotein I for the treatment of APS |
title_fullStr | Development of a high yield expression and purification system for Domain I of Beta-2-glycoprotein I for the treatment of APS |
title_full_unstemmed | Development of a high yield expression and purification system for Domain I of Beta-2-glycoprotein I for the treatment of APS |
title_short | Development of a high yield expression and purification system for Domain I of Beta-2-glycoprotein I for the treatment of APS |
title_sort | development of a high yield expression and purification system for domain i of beta-2-glycoprotein i for the treatment of aps |
topic | Methodology Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4650279/ https://www.ncbi.nlm.nih.gov/pubmed/26576675 http://dx.doi.org/10.1186/s12896-015-0222-0 |
work_keys_str_mv | AT mcdonnellthomas developmentofahighyieldexpressionandpurificationsystemfordomainiofbeta2glycoproteiniforthetreatmentofaps AT pericleouscharis developmentofahighyieldexpressionandpurificationsystemfordomainiofbeta2glycoproteiniforthetreatmentofaps AT laurineemmanuelle developmentofahighyieldexpressionandpurificationsystemfordomainiofbeta2glycoproteiniforthetreatmentofaps AT tommasirita developmentofahighyieldexpressionandpurificationsystemfordomainiofbeta2glycoproteiniforthetreatmentofaps AT garzagarciaacely developmentofahighyieldexpressionandpurificationsystemfordomainiofbeta2glycoproteiniforthetreatmentofaps AT gilesian developmentofahighyieldexpressionandpurificationsystemfordomainiofbeta2glycoproteiniforthetreatmentofaps AT ioannouyiannis developmentofahighyieldexpressionandpurificationsystemfordomainiofbeta2glycoproteiniforthetreatmentofaps AT rahmananisur developmentofahighyieldexpressionandpurificationsystemfordomainiofbeta2glycoproteiniforthetreatmentofaps |