Identification and characterization of a galactosyl peptide mimetic. Implications for use in removing xenoreactive anti-A Gal antibodies.

Journal Article

Gal alpha 1,3 Gal is thought to be the major antigenic epitope present on pig tissues to which XNAs bind. Removal of antibodies directed against that structure may be critical to the success of pig to human xeno-transplantation. As a first step toward the development of ligands capable of removing XNAs, we have used a phage-displayed peptide library to identify a six-amino-acid peptide that binds to the lectin GS-1-B4 (which binds the carbohydrate Gal alpha 1,3 Gal). This peptide blocks the binding of GS-1-B4 to pig aortic endothelial cells. The carbohydrate Gal alpha 1,3 Gal competes with the binding of GS-1-B4 to the peptide, suggesting that they may bind the same site. Using a RBC agglutination assay, we show that this peptide inhibits the agglutination of pig RBCs by heat-inactivated human serum at concentrations similar to that of Gal alpha 1,3 Gal.

Full Text

Duke Authors

Cited Authors

  • Kooyman, DL; McClellan, SB; Parker, W; Avissar, PL; Velardo, MA; Platt, JL; Logan, JS

Published Date

  • March 27, 1996

Published In

Volume / Issue

  • 61 / 6

Start / End Page

  • 851 - 855

PubMed ID

  • 8623148

Pubmed Central ID

  • 8623148

International Standard Serial Number (ISSN)

  • 0041-1337

Digital Object Identifier (DOI)

  • 10.1097/00007890-199603270-00001


  • eng

Conference Location

  • United States