| Autor: |
Bowditch RD; Committee on Vascular Biology, Scripps Research Institute, La Jolla, CA 92037., Tani PH, Halloran CE, Frelinger AL 3rd, McMillan R, Ginsberg MH |
| Jazyk: |
angličtina |
| Zdroj: |
Blood [Blood] 1992 Feb 01; Vol. 79 (3), pp. 559-62. |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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