Poster: Phytoremediation

Abs # 990: N- and O- linked glycosylation of endogenous proteins in Arabidopsis thaliana.

Presenter:	Shah, Miti M., mitimshah@hotmail.com
Authors	Shah, Miti M. (A)   Fujiyama, Kazuhito  (A)   Joshi, Lokesh  (A)
Affiliations:	(A): Arizona biodesign institute, Molecular and Cellular Biology, Arizona State University

Plants are emerging as a suitable host for the production of therapeutically important mammalian proteins. However, one of the shortcomings with the use of plants is a lack of fundamental knowledge regarding post-translational modifications (PTMs). PTMs hold keys to understanding the structure and functions of many proteins. Glycosylation is one of the most frequent and important post-translational modifications. Glycosylation serves many critical functions including cellular communication, half-life, structure and function of many glycoproteins. N- and O-linked glycosylation is common to many eukaryotic proteins, but species, organ and cell-type variations are known, each of which gives rise to different glycoforms of a polypeptide. Whether or not plants perform mammalian-like glycosylation is emerging as an important question in understanding the functionality of therapeutically important glycoproteins produced in plants. In studying the glycan structures of endogenous glycoproteins of Arabidopsis thaliana, we have discovered some previously unreported glycan motifs. Structural analyses of these glycans using lectin-blots, HPLC and mass spectrometric studies show that plants do possess the pathways and the potential to produce mammalian-like complex glycoforms on both N- and O-glycosylated proteins.