원문정보
초록
영어
N-glycosylation is a major post-translational protein modification, which alters physicochemical properties of the protein, affecting the folding, distribution, stability and thus biological function and efficiency of protein. β1,2-xylose and core α1,3-fucose residues on plant type complex N-glycans are potentially immunogenic in mammals. In this study, to remove the plant specific sugar residues and humanize the N-glycosylation in plant, we isolated mutants corresponding plant glycosyltransferase genes (N-acetylglucosaminyltransferaseI, N-acetylglucosaminyltransferaseII, α 1,3-fucosyltransferaseI, α1,3-fucosyltransferaseII, β1,2-xylosyltransferase, β 1,3-galactosyltransferase, α1,4-fucosyltransferase). Double, triple, quadruple and quintuple mutants were made by crossing the mutants and two quadruple mutants (fuct1/fuct2/xylt/gntII), (fuct1/fuct2/xylt/galt) are on the construction. The triple (fuct1/fuct2/xylt) and quadruple (fuct1/fuct2/xylt/fuct3), quintuple (fuct1/fuct2/xylt/fuct3/galt) mutants did not show significant developmental defects in a normal growth condition and they did not produce the plant specific sugar residues on the N-glycan. [Supported by BK21 program]