Molecular Cloning and Characterization of a Porcine UL16 Binding Protein (ULBP)-Like cDNA

Authors

Carmen N. Garcia-Borges, University of Arkansas for Medical Sciences, 151 Research, 4300 West 7th Street, Little Rock, Arkansas
Bounleut Phanavanh, University of Arkansas for Medical Sciences, 151 Research, 4300 West 7th Street, Little Rock, Arkansas
Sarika Saraswati, University of Arkansas for Medical Sciences, 151 Research, 4300 West 7th Street, Little Rock, Arkansas
Richard A. Dennis, University of Arkansas for Medical Sciences, 151 Research, 4300 West 7th Street, Little Rock, Arkansas
Mark D. Crew, University of Arkansas for Medical Sciences, 151 Research, 4300 West 7th Street, Little Rock, Arkansas

Date of this Version

2005

Comments

Published in Molecular Immunology 42 (2005) 665–671.

Abstract

UL16 binding proteins (ULBPs) are ligands for the NK cell activating receptor NKG2D. A cDNA encoding a porcine ULBP-like protein (PULBP) was cloned and the predicted amino acid sequence exhibited 35–52% identity to human ULBPs. Southern blot analysis suggested that there is only one ULBP-like gene in the pig genome. Transcripts of PULBP and another potential NKG2D ligand, MIC2, were detected by RT-PCR in a wide range of tissues. Recombinant PULBP-Fc and human ULBP2-Fc fusion proteins were made and used to examine PULBP binding to porcine PBMCs and a human NK cell line (NKL cells). PULBP-Fc bound to a subpopulation of porcine PBMCs but not NKL cells. Conversely, human ULBP2-Fc did not bind to porcine PBMCs but did stably interact with NKL cells.