Recognition of a carbohydrate xenoepitope by human NKRP1A (CD161)

Dale Christiansen, Effie Mouhtouris, Julie Milland, Alessandra Zingoni, Angela Santoni, Mauro S. Sandrin

Research output: Contribution to journalArticle


Background: Many immunologically important interactions are mediated by leukocyte recognition of carbohydrates via cell surface receptors. Uncharacterized receptors on human natural killer (NK) cells interact with ligands containing the terminal Galα(1,3)Gal xenoepitope. The aim of this work was to isolate and characterize carbohydrate binding proteins from NK cells that bind αGal or other potential xenoepitopes, such as N-acetyllactosamine (NAcLac), created by the deletion of α1, 3galactosyltransferase (GT) in animals. Methods and results: Initial analysis suggested the human C-type lectin NKRP1A bound to a pool of glycoconjugates, the majority of which contained the terminal Galα(1,3)Gal epitope. This was confirmed by high level binding of cells expressing NKRP1A to mouse laminin, which contains a large number of N-linked oligosaccharides with the Galα(1,3)Gal structure. The consequence of removing the terminal αGal was then investigated. Elevated NAcLac levels were observed on thymocytes from GT -/- mice. Exposing NAcLac on laminin, by α-galactosidase treatment, resulted in a significant increase in NKRP1A binding. Conclusions: NKRPIA binds to the αGal epitope. Moreover, exposing NAcLac by removal of αGal resulted in an increase in binding. This may be relevant in the later phases of xenotransplant rejection if GT -/- pigs, like GT -/- mice, display increased NAcLac expression.

Original languageEnglish
Pages (from-to)440-446
Number of pages7
Issue number5
Publication statusPublished - Sep 2006


  • α1,3galactosyltransferase knockout
  • Galα(1,3)Gal
  • N-acetyllactosamine
  • NKRP1A
  • Xenotransplantation

ASJC Scopus subject areas

  • Immunology

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