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CD94 and a novel associated protein (94AP) form a NK cell receptor involved in the recognition of HLA-A, HLA-B, and HLA-C allotypes.

Authors
  • Phillips, J H
  • Chang, C
  • Mattson, J
  • Gumperz, J E
  • Parham, P
  • Lanier, L L
Type
Published Article
Journal
Immunity
Publisher
Elsevier
Publication Date
Aug 01, 1996
Volume
5
Issue
2
Pages
163–172
Identifiers
PMID: 8769479
Source
Medline
License
Unknown

Abstract

Whereas the human killer cell inhibitory receptors (KIRs) for HLA class I are immunoglobulin-like monomeric type I glycoproteins, the murine Ly49 receptors for H-2 are type II homodimers of the C-type lectin superfamily. Here, we demonstrate that human NK cells also express C-type lectin receptors that influence recognition of polymorphic HLA-A, HLA-B, and HLA-C molecules. These receptors are heterodimers composed of CD94 chains covalently associated with novel tyrosine-phosphorylated glycoproteins (94AP). Some NK clones recognize a common HLA-C ligand using both KIRs and CD94-94AP receptors. These findings suggest the existence of human inhibitory MHC class I receptors of the immunoglobulin and C-type lectin superfamilies and indicate overlap in ligand specificity.

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