Abstract:
BACKGROUND:According to Landsteiner's law, alloantibodies are prevalent and autoantibodies are absent in the ABO blood group system. However, one study (Spalter et al., Blood 1999;93:4418-24) has suggested that low-affinity ABO autoantibodies, mitigated by anti-idiotypic immunoglobulins are also prevalent, while another publication (Rieben et al., Eur J Immunol 1992;22:2713-7) shows that humans do not have B-lymphocytes capable of producing immunoglobulin G ABO autoantibodies. STUDY DESIGN AND METHODS:We used hapten-specific chromatography to isolate allo- and autoantibodies from pools of A or B serum and then characterized the resultant antibodies against a wide range of ABO and related glycoconjugates. RESULTS:We found that the apparent autoantibodies are directed against blood group A or B disaccharides, without consideration for the presence of fucose, but requiring the absence of elongating sugar X in composition of Gal(NAc)α1-3(Fucα1-2)Galβ1-X-terminated carbohydrate chain. In contrast, ABO alloantibodies required a minimum trisaccharide Gal(NAc)α1-3(Fucα1-2)Gal epitope and recognize the elongated type-specific tetrasaccharides. Furthermore, alloantibodies appear to be a small set of specific yet crossreactive antibodies that detect all backbone types of A or B antigens, rather than being a collection of specific antibodies, each of which detects a different type of A or B antigen. CONCLUSION:Apparent ABO autoantibodies appear to have no natural human target.
journal_name
Transfusionjournal_title
Transfusionauthors
Obukhova P,Korchagina E,Henry S,Bovin Ndoi
10.1111/j.1537-2995.2011.03381.xsubject
Has Abstractpub_date
2012-04-01 00:00:00pages
860-9issue
4eissn
0041-1132issn
1537-2995journal_volume
52pub_type
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