PubMed · 7349298
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B Beiguelman. 1981. Genetic polymorphic systems and Hanseniasis.. https://pubmed.ncbi.nlm.nih.gov/7349298/
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A new neoglycolipid (AgH-1) bearing carbohydrate units that mimics the antigenic determinant of the O-blood group was synthesized and the effect of its incorporation in dipalmitoylphosphatidylcholine (DPPC): cholesterol liposomes was evaluated. The results obtained show that AgH-1 is readily incorporated into DPPC:cholesterol liposomes. The conditions leading to the optimal incorporation are the result of a compromise between incorporation efficiency and incorporation extent. The presence of AgH-1 produces liposomes of smaller size, with only small changes in the properties of the bilayer. However, the data obtained employing diphenylhexatriene and laurodan as fluorescence probes and merocyanine 540 as optical probe suggest that AgH-1 incorporation leads to a small rigidization of the liposomes at temperatures lower than ca. 42 degrees C.
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BACKGROUND: Cromer blood group antigens are located on decay-accelerating factor (DAF, CD55), which contains four short consensus repeats (SCRs). Cromer system antibodies may be of clinical significance in blood transfusion. STUDY DESIGN AND METHODS: Soluble recombinant DAF (srDAF) constructs, consisting of all four SCRs or of only two SCRs, were expressed in the yeast Pichia pastoris. They are used in hemagglutination-inhibition tests with Cromer system antibodies and with DAF-specific monoclonal antibodies. RESULTS: The srDAF inhibited hemagglutination by all Cromer system alloantibodies in undiluted serum. Antibodies to antigens of other blood group systems were not inhibited by the srDAF. Hemagglutination-inhibition tests with domain-deleted srDAF showed that UMC is on SCR-4 and confirmed that Tca, TcaTcb, and WESb are on SCR-1; Dra is on SCR-3; and Cra is on SCR-4. CONCLUSIONS: Hemagglutination inhibition with srDAF is useful in the recognition of antibodies that belong to the Cromer blood group system and facilitates pretransfusion testing. This use of domain-deleted srDAF provides an easy method of determining epitope location on DAF and is an aid to more precise identification of Cromer system antibodies.