ABO Polymorphism & Diet
Within the gene, at the nucleotide sequence level, the differences among individuals with different human ABO alleles are minimal with only minor substitutions and deletions/insertions. These differences result in changes in the gene-encoded proteins: A and B glycosyltransferases and non-functional O proteins. The specificity and activity of the glycosyltransferases encoded by weak and rare A and B subgroup alleles, as well as cis-AB and B(A) alleles that specify the expression of both A and B antigens by single genes, are modified. The functional enzymes, A and B transferases, are involved in the biosynthesis of the oligosaccharide A and B antigens, respectively.
Because these antigens are expressed on the epithelial cells of gastrointestinal tract, in addition to red blood cells (RBCs), it is theoretically possible that these antigens may interact with carbohydrate-recognizing proteins like lectins present in the diet. Because A and B antigens are carried on glycoproteins and glycolipids on the cell surface, they may also modify the functions of those glycoconjugates.
ABH antigens are not restricted to the humans, but they are also present in nature. Therefore, it is possible that A/B antigens in the diet may also interact, within the human body, with naturally occurring antibodies against those antigens and/or with lymphocytes that carry those antibodies, in addition to the carbohydrate-binding proteins.
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