LACK OF BINDING OF PEPTIDES CARRYING THE HUMAN PLATELET ANTIGEN-1 (HPA-1) DIMORPHISM TO PURIFIED HLA-DRW52A MOLECULES

被引：5

作者：

BRAUD, V ^{[1
]}

VALENTIN, N ^{[1
]}

CHOPPIN, J ^{[1
]}

CESBRON, A ^{[1
]}

BIGNON, JD ^{[1
]}

BLANCHARD, D ^{[1
]}

MULLER, JY ^{[1
]}

机构：

[1] INSERM, U152, F-75014 PARIS, FRANCE

来源：

REVUE FRANCAISE DE TRANSFUSION ET D HEMOBIOLOGIE | 1993年 / 36卷 / 05期

关键词：

D O I：

10.1016/S1140-4639(05)80156-X

中图分类号：

R5 [内科学];

学科分类号：

1002 ; 100201 ;

摘要：

The strong association between anti-HPA-1a alloimmunization and DR3, DRw52a phenotype in HPA-1b homozygous women suggests that these class II molecules play a crucial role in the immune response against HPA-1a. The diallelic system HPA-1 results in a single amino acid polymorphism at the residue 33 of the glycoprotein IIIa, So, we tested the binding of peptides from the 25-42 region of the GPIIIa to purified HLA-DR3 and -DRw52a molecules, using a solid phase assay and a liquid phase peptide binding assay. No binding was demonstrated, indicating that either the crucial region for binding to class II molecules is not the 25-42 region, or that other events only occurring << in vivo >> are required for binding. These results may also suggest an indirect role of the residue 33 for T-cell stimulation.

引用

页码：439 / 449

页数：11

共 33 条

[31] AN OPTIMAL VIRAL PEPTIDE RECOGNIZED BY CD8+ T-CELLS BINDS VERY TIGHTLY TO THE RESTRICTING CLASS-I MAJOR HISTOCOMPATIBILITY COMPLEX PROTEIN ON INTACT-CELLS BUT NOT TO THE PURIFIED CLASS-I PROTEIN [J].