Molecular cloning and characterisation of the CD18 partner in ovine (Ovis aries) beta2-integrins.
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.
Zecchinon
L
L
Department of Pathology, Faculty of Veterinary Medicine, University of Liège, FMV Sart Tilman B43, B-4000 Liège, Belgium.
Fett
T
T
Baise
E
E
Desmecht
D
D
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D018821:CD18 Antigens / Q000235:genetics*; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D034561:Sheep, Domestic / Q000235:genetics*
D018821:CD18 Antigens; D018076:DNA, Complementary