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Determination of inauthentic glycosylation in transgenic plants

Project Code: G03029;
Publication:

Tryfona, T., Liang, H.-C., Kotake, T., Kaneko, S., Marsh, J., Ichinose, H., Lovegrove, A., Tsumuraya, Y., Shewry, P.R., Stephens, E. & Dupree, P. (2011) Carbohydrate structural analysis of wheat flour arabinogalactan protein. Carbohydrate Research 345, 2648-2656, published online doi:10.1016/j.carres.2010.09.018
Marsh, J.T., Tryfona, T., Powers, S.J., Stephens, E., Dupree, P., Shewry, P.R. & Lovegrove, A. (2011) Determination of the N-glycosylation patterns of seed proteins: applications to determine authenticity and the substantial equivalence of GM crops. J. Agric. Food Chem., 59 (16), 8779-8788, doi: 10.1021/jf2010854

04/01/2012

Rothamsted Research
Shewry, P ;
University of Cambridge
Dupree, P

The main aims of project GO3029 was the development of methods to identify and characterise N- and O-linked glycans on plant proteins to determine whether proteins expressed in transgenic plants are inauthentically glycosylated.
Methods developed and evaluated at the University of Cambridge were successfully transferred to Rothamsted Research where they were applied to transgenic and non-transgenic plants. These included the transgenic pea lines expressing the bean -amylase inhibitor (Prescott et al. 2005) which had caused public concern when they were used in animal feeding studies and found to produce an altered immune response, compared to the native bean α-amylase inhibitor.
The N-glycosylation methods developed at the University of Cambridge were reduced to a Standard Operating Procedure (SOP) at Rothamsted Research suitable for routine use in industry and by regulatory authorities.

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