Post translational modifications are described as enzymatic and covalent chemical reactions that modify the polypeptide chain formed after translation of mRNA. Some of these include phosphorylation, glycosylation, ubiquination, methylation, acetylation, etc. Animal, plant, fungi and bacterial cell systems all have the ability to undergo modifications in their proteins. Though with increase in the complexity of their cellular organization, many similarities are observed in midst of the differences in their post translational modifications. Glycosylation is the addition of different sugar molecules at specific amino acid residues of translated polypeptide chain. In glycosylation mechanisms, there are significant variations in terms of monosaccharides used and the structures formed due to different repertoires of glycosidases and glycosyltransferases. So far, there have been numerous studies on mammalian and yeast glycoproteins, but less is known about the synthesis and structural variation of their plant counterparts. As transgenic plants have emerged as large-scale producers of recombinant proteins, the need for humanization of glycosylated protein has increased. In the present study Protein Glycosylation in plants is discussed with highlights on how they differ from the mammalian and yeast Glycosylation pathways and description is given on the ways to humanize plant-made recombinant proteins.
Name of the Student: M. Shruthika
Reg No: 1741210001
Batch: M.Tche II year
Name of the Guide : Dr. M. Parani