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Altered glycosylation leads to Tr polyagglutination
G R Halverson1, A H Lee, R Øyen
1From the New York Blood Center, New York, New York.
Transfusion
|October 27, 2004
Summary
Polyagglutination, a condition where red blood cells (RBCs) react with most adult sera, was identified in an infant with a rare genetic defect. This defect involves altered glycosylation, leading to exposed sugars on RBCs.
Area of Science:
- Hematology
- Biochemistry
- Genetics
Background:
- Polyagglutination involves red blood cells (RBCs) agglutinated by adult sera but not cord sera.
- Associated with infections, myeloproliferative, and myelodysplastic disorders.
- Lectins are used to identify polyagglutination.
Observation:
- A Hispanic infant presented with hemolytic anemia, Bernard-Soulier-like syndrome, neutropenia, and developmental delays.
- The patient's Group O RBCs showed polyagglutination with sera and lectins, but not cord sera or specific lectins.
- RBC membrane analysis revealed reduced glycophorins A and B and altered Band 3 mobility.
Findings:
- Reduced N-acetylneuraminic acid on RBC N- and O-glycans, exposing specific galactosidases.
- Suggests an altered glycosyltransferase causing defective glycosylation in RBCs and other cells.
- This unique polyagglutination pattern was designated Tr.
Implications:
- Highlights a novel genetic basis for polyagglutination.
- Underscores the role of glycosylation in RBC membrane integrity and function.
- Provides insights into rare genetic disorders affecting glycosylation pathways.