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Localization of a PlA1 epitope to the amino terminal 66 residues of platelet glycoprotein IIIa

Academic Article
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Overview

authors

  • Bowditch, R. D.
  • Tani, P. H.
  • Halloran, C. E.
  • Frelinger, A. L.
  • Mc Millan, Robert
  • Ginsberg, Mark

publication date

  • February 1992

journal

  • Blood  Journal

abstract

  • A platelet glycoprotein (GP) IIIa epitope library was constructed by insertion of randomly cleaved GPIIIa cDNA fragments in the prokaryotic expression vector lambda gt22 and screened with purified anti-PlA1 antibodies for clones expressing a PlA1 epitope. Five independent clones were isolated and characterized by nucleotide sequencing. The smallest anti-PlA1 reactive clone obtained encoded the amino terminal 66 residues of mature GPIIIa. Substitution of leucine33 (PlA1) with a proline33 (PlA2) by in vitro mutagenesis resulted in the loss of anti-PlA1 reactivity; however, this clone still reacted with anti-GPIIIa polyclonal antibodies. These data indicate that a PlA1 alloantigenic epitope is located within a small, unglycosylated fragment of GPIIIa containing the polymorphism responsible for the PIA phenotype. Furthermore, these results prove that small recombinant mimics of a PlA1 epitope may be synthesized and used for detection of these alloantibodies.

subject areas

  • Alleles
  • Amino Acid Sequence
  • DNA Mutational Analysis
  • Epitopes
  • Humans
  • Molecular Sequence Data
  • Phenotype
  • Platelet Membrane Glycoproteins
  • Recombinant Proteins
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Identity

International Standard Serial Number (ISSN)

  • 0006-4971

PubMed ID

  • 1370635
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Additional Document Info

start page

  • 559

end page

  • 562

volume

  • 79

issue

  • 3

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