Subtle Differences: Therapeutic Antibodies Vary Depending on Production System
High-precision analysis by the University of Natural Resources and Life Sciences, Vienna uncovers differences in recombinantly produced immunoglobulins; process also affects stability
(firmenpresse) - Vienna, 10 July 2018 parison of the structural properties of antibody isotopes that were manufactured in cell cultures or plants. Equipment BOKU (EQ BOKU) based at the University of Natural Resources and Life Sciences, Vienna (BOKU) employed state-of-the-art mass spectrometers to pinpoint minute differences in the glycosylation of immunoglobulins.
Antibodies are one of the most precise forms of medicine and are increasingly being used to combat cancer and other conditions. They are frequently produced recombinantly, with a range of different manufacturing processes in use. Each process creates an identical protein scaffold in the antibody, but there are differences in what is known as glycosylation, or modification by adding specific carbohydrates. Previously, little was known about the way in which these differences come about and the form they take. Identifying these subtle, but potentially medically significant distinctions requires extremely complex analysis, which is only possible using the latest mass spectrometry procedures. A BOKU team had access to such equipment at the university
Getting to the heart of the matter
The team headed by Prof. Richard Strasser is the first to identify precise differences in the glycosylation patterns of immunoglobulin A, which had been produced either in human cell cultures (HEK293) or plant systems (Nicotiana benthamiana). Prof. Strasser, a member of the Department of Applied Genetics and Cell Biology, commented:
With the help of ultra-modern techniques called capillary reversed-phase chromatography and electrospray mass spectrometry provided by EQ, the team managed to analyse glycosylation in each system down to the finest detail. They found that the immunoglobulin A produced in the HEK293 cell culture had many more and also more complex N-glycans
Bonding
Although the glycosylations in the antibodies produced in N. benthamiana were purely plant-specific, the antibodies displayed the same bonding properties for antigens as those manufactured using human cells. This suggests that as far as therapeutic applications are concerned, the choice of production system makes no difference. However, further analysis by Prof. Strasser
His team has all the necessary resources to do just that at EQ BOKU. Cutting-edge mass spectrometers, chromatography procedures and calorimeters
About EQ-BOKU
EQ-BOKU provides low-cost access to state-of-the-art equipment to research institutes, companies, and universities. EQ-BOKU equipment and expertise is particularly suited to projects in the following areas: chemistry, biochemistry, genetics, cell biology, molecular biology, biotechnology, nanobiotechnology, bioinformatics, food science, enzyme technology, water and sewage. EQ-BOKU VIBT is an independent subsidiary of the University of Natural Resources and Life Sciences, Vienna. W: http://eq-vibt.boku.ac.at/
Enquiries:
Scientific Contact:
Prof. Richard Strasser
Department for Applied Genetics and cell Biology
University of Natural Resources and Life Sciences, Vienna
Muthgasse 18
1190 Vienna, Austria
T +43 / 1 / 47654-94145
E richard.strasser(at)boku.ac.at
W http://www.boku.ac.at/
EQ-BOKU GmbH
Ingrid D
Muthgasse 18
1190 Vienna, Austria
T +43 / 1 / 47654
E ingrid.doeller-diem(at)boku.ac.at
W http://eq-vibt.boku.ac.at/
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Datum: 10.07.2018 - 04:47 Uhr
Sprache: Deutsch
News-ID 1538310
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Typ of Press Release: Erfolgsprojekt
type of sending: Veröffentlichung
Date of sending: 10.07.2018
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