Glycobiology Advance Access originally published online on January 3, 2003
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Glycobiology, 2003, Vol. 13, No. 4 279-284
© 2003 Oxford University Press
Specificity of human anti-NOR antibodies, a distinct species of "natural" anti-
-galactosyl antibodies
2 Department of Immunochemistry, Ludwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Rudolf Weigl St. 12, 53-114 Wroclaw, Poland
3 Department of Chemistry, Swedish University of Agricultural Sciences, S-750 07 Uppsala, Sweden
4 Laboratory of Carbohydrate Chemistry, Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, v-437 Moscow, Russian Federation
Received on August 26, 2002; revised on November 27, 2002; accepted on November 28, 2002
Natural anti-NOR antibodies are common in human sera and agglutinate human erythrocytes of a rare NOR phenotype. The NOR phenotype-related antigens are unique neutral glycosphingolipids recognized by these antibodies and Griffonia simplicifolia IB4 isolectin (GSL-IB4). The oligosaccharide chains of NOR glycolipids are terminated by Gal
1-4GalNAcß1-3Gal units. To characterize the specificity of anti-NOR antibodies and compare it with specificities of GSL-IB4 and known anti-Gal1,3Gal antibodies, -galactosylated saccharides and saccharide-polyacrylamide conjugates were used. New synthetic oligosaccharides, corresponding to the terminal di- and trisaccharide sequence of NOR glycolipids and the conjugate of the NOR-tri with HSA were included. These compounds were tested by microtiter plate ELISA and hemagglutination inhibition. Anti-NOR antibodies reacted most strongly with Gal1-4GalNAcß1-3Gal (NOR-tri), and over 100 times less strongly with Gal1-4GalNAc (NOR-di). The antibodies reacted also with Gal1-4Gal and Gal1-4Galß1-4GlcNAc, similarly as with NOR-di but not with other tested compounds. In turn, anti-Gal1,3Gal antibodies reacted most strongly with Gal1-3Gal and were very weakly inhibited by the NOR-related oligosaccharides (weaker than by galactose), and NOR-tri was less active than NOR-di. GSL-IB4 reacted with all tested -galactosylated saccharides and conjugates, including the similarly active NOR-tri and NOR-di. These results showed that anti-NOR represent a new species of anti--galactosyl antibodies with high affinity for the Gal1-4GalNAcß1-3Gal sequence present in rare NOR erythrocytes.
1 To whom correspondence should be addressed; e-mail: lisowska{at}iitd.pan.wroc.pl
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