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A human monoclonal antibody specific for the leucine-33 (P1A1, HPA-1a) form
of platelet glycoprotein IIIa from a V gene phage display library
HM Griffin and WH Ouwehand
Division of Transfusion Medicine, University of Cambridge, UK.
IgG alloantibodies to polymorphic platelet glycoproteins (GPs) are known to
be responsible for severe thrombocytopenia in the neonate and after
transfusion. Platelet GPIIIa can have either a leucine or a proline at
residue 33. The most immunogenic platelet alloantigen in thrombocytopenia
is the leucine 33 form of GPIIIa. Here, we have generated human monoclonal
antibody fragments that are specific for the leucine and not the proline
form of GPIIIa and can inhibit the binding of polyclonal human IgG
alloantibodies to GPIIIa leucine 33 on platelets. The antibody fragments
were selected from a library of single chain Fv fragments displayed on the
surface of filamentous phage. The VH gene repertoire was derived from the
peripheral blood lymphocytes of an alloimmunized individual and recombined
with a VL gene repertoire from a nonimmune source. Antibodies such as
these, which are able to distinguish between two variant forms of a native
antigen and which have been unobtainable by conventional hybridoma
technology, have both diagnostic and potential therapeutic applications.
Volume 86,
Issue 12,
pp. 4430-4436,
12/15/1995
Copyright © 1995 by The American Society of Hematology
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