Affiliations: Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria
Correspondence:
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Corresponding author: Herta Steinkellner, Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria. Tel.: +43 1 47654 6700; Fax: +43 1 47654 6392; E-mail:herta.steinkellner@boku.ac.at
Abstract: Human immunoglobulins circulate as highly heterogeneously glycosylated
mixture of otherwise homogeneous protein backbones. A series of studies,
mainly on IgG, have unequivocally proven that antibodies modulate their
effector function through sugars present in the Fc domain. However, our
limited technology in producing complex proteins such as antibodies, with
defined glycan structures hamper in depths studies. This review introduces a
plant based expression platform enabling engineering of antibody glycans.
The procedure is based on the simultaneous delivery of appropriate
constructs, carrying cDNAs of target proteins (e.g. heavy and light chain of
antibodies) in combination with human glycosylation enzymes into plant
leaves. Harvesting of recombinant proteins one week post construct delivery
allows high speed and flexibility. Major achievements include the production
of functional active slialylated pentameric IgMs in tobacco leaves. The
system provides a viable approach to the generation of antibodies with
defined glycoforms on demand, contributing to studies on antibody glycans
and the development of novel antibody based drugs.
