Transgenic approaches for the reduction of Galalpha(1,3)Gal for xenotransplantation.
The major barrier to clinically successful xenotransplantation is the lack of effective therapies aimed at eliminating antibody and complement -dependent hyperacute rejection. This review examines transgenic strategies to eliminate or reduce expression of the major pig to human xenoantigen Galalpha(1,3)Gal such that the epitope is no longer recognized by natural human antibodies, by the use of glycosidases and/or glycosyltransferases that can competitively and effectively inhibit the activity of the alpha1,3galactosyltransferase gene and thereby eliminate the xenoantigen Galalpha(1,3)Gal.
Sandrin
M S
MS
Molecular Immunogenetics Laboratory Austin Research Institute Austin & Repatriation Medical Center Heidelberg Vic. 3084 Australia. ms_sandrin@muwayf.unimelb.edu.au
Osman
N
N
McKenzie
I F
IF
D000818:Animals; D030801:Animals, Genetically Modified; D015478:Antigens, Heterophile / Q000276:immunology / Q000378:metabolism*; D004187:Disaccharides / Q000276:immunology* / Q000378:metabolism; D000939:Epitopes / Q000378:metabolism; D005647:Fucosyltransferases / Q000235:genetics / Q000378:metabolism; D005700:Galactosyltransferases / Q000378:metabolism; D006084:Graft Rejection / Q000276:immunology; D006801:Humans; D013552:Swine / Q000276:immunology; D019076:Transgenes; D014183:Transplantation, Heterologous; D000519:alpha-Galactosidase / Q000235:genetics / Q000378:metabolism; D000097631:Galactoside 2-alpha-L-fucosyltransferase
D015478:Antigens, Heterophile; D004187:Disaccharides; D000939:Epitopes; D005647:Fucosyltransferases; D005700:Galactosyltransferases; D000519:alpha-Galactosidase; D000097631:Galactoside 2-alpha-L-fucosyltransferase; C055075:galactosyl-(1-3)galactose; C047006:N-acetyllactosaminide alpha-1,3-galactosyltransferase