Solid phase measurements of antibody and lectin binding to xenogenic carbohydrate antigens
Research output: Contribution to journal › Journal article › Research › peer-review
OBJECTIVES: In future pig-to-man xenotransplantation it is important to master tools that identify potentially xenogenic alphagalactose (Galalpha) antigens in the doner tissue. DESIGN AND METHODS: We have measured the binding potentials of Galalpha detecting lectins and antibodies, including a naturally occurring subfraction from human serum, to Galalpha containing neoglycoproteins and mouse laminin that were immobilized on microtiter plates. RESULTS: Galalpha reactive antibodies with similar monosaccharide specificity have distinct structural preference for sugar ligands. Laminin and neoglycoproteins were treated with alpha-galactosidase and subsequently incubated with antibodies and lectins. The enzyme treatment was more deleterious on antibody binding than on lectin binding. CONCLUSION: Antibodies and lectins may bind to different galactose determinants on the glycoproteins. Two anti-Galalpha1 antibodies that both have been raised against glycans on rabbit red blood cells may recognize Galalpha-antigens with varying specificities. Binding results obtained after digestion with alpha-galactosidase indicate that some xenoreactive Galalpha groups are not directly accessible for removal by the enzyme.
Original language | English |
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Journal | Clinical Biochemistry |
Volume | 37 |
Issue number | 1 |
Pages (from-to) | 36-41 |
Number of pages | 5 |
ISSN | 0009-9120 |
Publication status | Published - 2004 |
Bibliographical note
Keywords: Animals; Antibodies; Antigens; Galactose; Glycoproteins; Humans; Laminin; Mice; Plant Lectins; Protein Binding; alpha-Galactosidase
ID: 10025871