The leukocyte integrins play a critical role in a number of cellular adhesive interactions during the immune response. We describe here the isolation and characterization of the ovine beta(2) (CD18) subunit, common to the leukocyte beta(2)-integrin family. The deduced 770-amino-acid sequence reveals a transmembrane protein with 81%, 83% and 95% identity with its murine, human and bovine homologues, respectively. Comparisons of CD18 sequences emphasize the functional importance of the beta(2) subunit I-like domain and included metal ion-dependent adhesion site (MIDAS)-like motif and confirm that of the cytoplasmic tail. The data provided here will offer the possibility to explore new avenues in studies based on the ovine model.
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