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    The isolation and characterisation of antiplatelet antibodies.

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    Publication date
    2006
    Author
    Lindsey, Nigel J.
    Behrendt, M.
    Hamidpour, M.
    Partridge, L.J.
    Griffiths, B
    Keyword
    Autoimmune thrombocytopenia purpura
    Fab antiplatelet antibody
    Library phage
    Platelet function
    Peer-Reviewed
    Yes
    
    Metadata
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    Abstract
    The isolation and characterisation of antiplatelet antibodies in autoimmune thrombocytopenia purpura patients (ITP) is described. Autoimmune thrombocytopenia purpura is an autoimmune disease, clinically defined by low platelet counts, normal or increased megakaryocytopoiesis and antiplatelet antibodies in serum. This study used phage display to isolate Fab antiplatelet antibodies to study the structure-function relationships of pathogenic antibodies in ITP. Out of six randomly selected colonies, four colonies reacted strongly with whole platelets in enzyme-linked immunosorbent assay (ELISA). Sequence analysis showed that all four colonies had the same DNA sequence and were the same antibody. Results of Western blotting against non-reduced human platelet lysate showed that the Fab reacted with platelet proteins with apparent molecular weights of 116, 92 and 39 kD. Furthermore, Western blotting assay against purified membrane glycoprotein IIIa demonstrated reactivity against a band with a molecular weight of 92 kD. Results from Western blotting against platelet lysate and pure platelet glycoprotein confirmed the Fab fragment recognised the platelet glycoprotein IIIa. Three out of the four phage colonies produced soluble Fab, which demonstrated reactivity against platelet autoantigens in ELISA. Further sequence analysis showed that the Fab was somatically mutated suggesting antigen drive and therefore T-cell assistance was important in the development of this antibody. One of the somatic mutations introduced an RSD amino acid sequence in the complementary determining region 1(CDR1) of the light chain, which may mimic the RGD motif of fibrinogen which binds integrin GPIIb/IIIa. This raises the possibility that somatic mutation and antigen drive have produced a pathogenic autoantibody.
    URI
    http://hdl.handle.net/10454/2839
    Version
    No full-text available in the repository
    Citation
    Lindsey, N.J., Behrendt, M., Hamidpour, M. and Partridge, L et al. (2006). The isolation and characterisation of antiplatelet antibodies. European Journal Of Haematology. Vol. 76, No. 4, pp. 331-338.
    Link to publisher’s version
    http://www3.interscience.wiley.com/cgi-bin/fulltext/118553399/PDFSTART
    Type
    Article
    Collections
    Engineering and Informatics Publications

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