Glycobiology Advance Access published online on September 1, 2004
Glycobiology, doi:10.1093/glycob/cwh146
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1 Department of Immunochemistry, Ludwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Rudolf Weigl St. 12, 53-114 Wroclaw, Poland
* To whom correspondence should be addressed. E-mail: lisowska{at}iitd.pan.wroc.pl.
The rare NOR erythrocytes, which are agglutinated by most human sera, contain unique glycosphingolipids (globoside elongation products) terminating with the sequence Gal
Revised August 30, 2004
Accepted August 30, 2004
ORIGINAL ARTICLES
Anti-
-galactosyl antibodies recognizing epitopes terminating with 1,4-linked galactose: human ‘natural’ and mouse monoclonal anti-NOR and anti-P1 antibodies
nierz-Alejska 2,
2 Institute of Hematology and Blood Transfusion, 00-957 Warsaw, Poland
3 Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, v-437 Moscow, Russian Federation
4 Regional Center for Blood Transfusion, 50-345 Wroclaw, Poland
Abstract 
1-4GalNAc
1-3Gal- recognized by common natural human antibodies. Anti-NOR antibodies were isolated from several human sera by affinity procedures and their specificity was tested by inhibition of antibody binding to NOR-tri-polyacrylamide (PAA) conjugate (ELISA) by the synthetic oligosaccharides, Gal1-4GalNAc1-3Gal (NOR-tri), Gal1-4GalNAc (NOR-di), Gal1-4Gal1-3Gal1-4Glc ((Gal)3Glc), and Gal1-4Gal (P1-di). Two major types of subspecificity of anti-NOR antibodies were found. Type 1 antibodies were found to react strongly with (Gal)3Glc and NOR-tri, and weakly with P1-di and NOR-di, which indicated specificity for the trisaccharide epitope Gal1-4Gal/GalNAc1-3Gal. Type 2 antibodies were specific to Gal1-4GalNAc, since they were inhibited most strongly by NOR-tri and NOR-di and were not (or very weakly) inhibited by (Gal)3Glc and P1-di. Monoclonal anti-NOR antibodies were obtained by immunizing mice with NOR-tri-HSA and were found to have type 2 specificity. All anti-NOR antibodies reacted specifically with NOR glycolipids on thin-layer plates. The cross-reactivity of type 1 anti-NOR antibodies with Gal1-4Gal drew attention to a possible antigenic relationship between NOR and blood group P system glycolipids. The latter glycolipids include Pk (Gal1-4Gal1-4Glc-Cer) present in all normal erythrocytes, and P1 (Gal1-4Gal1-4GlcNAc1-3Gal1-4Glc-Cer) present only in P1 erythrocytes. Sera of some P2 (P1-negative) persons contain natural anti-P1 antibodies. This prompted us to test the specificity of anti-P1 antibodies. Natural human anti-P1 isolated from serum of P2 individual and mouse monoclonal anti-P1 were best inhibited by Gal1-4Gal1-4GlcNAc (P1-tri), and did not react with NOR-tri and NOR-di. Monoclonal anti-P1 bound to pk and P1 glycolipids, and not to NOR glycolipids. These results indicated an entirely different specificity of anti-NOR and anti-P1 antibodies. Human serum samples differed in the content of anti--galactosyl antibodies, including both types of anti-NOR. In the sera of some individuals, type 1 or type 2 anti-NOR antibodies dominated, and other samples contained mixtures of both types of anti-NOR. The biological significance of these new abundant anti--galactosyl antibodies still awaits elucidation.-galactosyl; anti-NOR; anti-P1; glycolipids; polyagglutination.
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  M. Duk, S. Singh, V. N. Reinhold, H. Krotkiewski, E. Kurowska, and E. Lisowska Structures of unique globoside elongation products present in erythrocytes with a rare NOR phenotype Glycobiology, March 1, 2007; 17(3): 304 - 312. [Abstract] [Full Text] [PDF]
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