Abstract
1% of circulating IgG in man is anti-Gal antibody, which interacts specifically with the carbohydrate structure Galα1→3Galβ1→GlcNAc-R on mammalian glycoconjugates (described throughout as the α-galactosyl epitope). This epitope is abundant on cell surface glycoconjugates of non-primate mammals, prosimians, and New World monkeys. It is not found on cells of Old World monkeys, apes, and man because of diminished α1→3 galactosyltransferase enzyme activity. However, the α1→3 galactosyltransferase gene seems to be present within the human genome. A mechanism that increases α1→3 galactosyltransferase activity in human cells could trigger an autoimmune process mediated by anti-Gal binding to the newly synthesised α-galactosyl epitopes.
Published Version
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