A mAb recognizing a 40- to 44-kDa monomeric molecule on the surface of
chicken T cells was used to screen a cDNA expression library made fro
m Con A-stimulated chicken spleen cells. The sequence of the cDNA obta
ined encoded a molecule having 50% amino acid sequence identity with m
ammalian CD28, but the cysteine residue involved in the inter-chain br
idge of the mammalian CD28 homodimer was not conserved in the chicken
sequence. The molecule produced in transfected COS-7 cells was also re
cognized by another mAb that had previously been thought to recognize
an avian homologue of CD2. The sequence data establish that this molec
ule is a homologue of mammalian CD28 in the strict evolutionary sense.