Development of a high yield expression and purification system for Domain I of Beta-2-glycoprotein I for the treatment of APS
Author(s)
Type
Journal Article
Abstract
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.
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.
Date Issued
2015-11-14
Date Acceptance
2015-11-03
Citation
BMC Biotechnology, 2015, 15 (1)
ISSN
1472-6750
Publisher
BioMed Central
Journal / Book Title
BMC Biotechnology
Volume
15
Issue
1
Copyright Statement
© 2015 McDonnell et al. This 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.
Identifier
http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000364766600001&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
Subjects
Science & Technology
Life Sciences & Biomedicine
Biotechnology & Applied Microbiology
Antiphospholipid syndrome
Protein production
Inclusion bodies
E. Coli
Beta-2-Glycoprotein I
Domain I
Automated
ANTIPHOSPHOLIPID ANTIBODIES
ESCHERICHIA-COLI
ANTICARDIOLIPIN ANTIBODIES
BETA(2)-GLYCOPROTEIN I
RHEUMATOID-ARTHRITIS
CERTOLIZUMAB PEGOL
PROTEIN-PRODUCTION
REFRACTORY GOUT
GLYCOPROTEIN-I
URATE OXIDASE
Publication Status
Published
Article Number
104
Date Publish Online
2015-11-14