Relationship of the human erythrocyte Wrb antigen to an interaction between glycophorin A and band 3.

Journal Article (Journal Article)

The Wrb antigen is a high-frequency human erythrocyte antigen invariably absent from En (a-) erythrocytes, which lack glycophorin A. However, glycophorin A from En (a+) Wr (a+b-) red cells has an amino acid sequence identical to that of glycophorin A from Wr (b+) erythrocytes. Evidence has suggested that the Wrb antigen may require the interaction of glycophorin A with either a lipid moiety or with another erythrocyte-integral membrane protein, band 3. We have investigated the role of band 3 in Wrb expression using murine monoclonal antibodies (MoAbs) with Wrb specificity. These antibodies reacted by radioimmunoassay (RIA) only with cells expressing both glycophorin A and band 3. In immunoprecipitation studies, Wrb antibodies immunoprecipitated both band 3 and glycophorin A, while antibodies specific for band 3 or glycophorin precipitated only the protein with which they were reactive. These data strongly suggest that band 3 is the other membrane component necessary for expression of Wrb and that band 3 and glycophorin A are closely associated in the erythrocyte membrane.

Full Text

Duke Authors

Cited Authors

  • Telen, MJ; Chasis, JA

Published Date

  • August 15, 1990

Published In

Volume / Issue

  • 76 / 4

Start / End Page

  • 842 - 848

PubMed ID

  • 2383660

International Standard Serial Number (ISSN)

  • 0006-4971


  • eng

Conference Location

  • United States