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*
Turku Immunology Centre and Department of Medical Microbiology, Turku University, Turku, Finland;
Basel Institute for Immunology, Basel, Switzerland; and
Institute for Animal Health, Compton, United Kingdom
The chicken CD5 cDNA was isolated by COS cell expression cloning
utilizing a novel mAb 2-191. The cDNA contains a 1422-nucleotide open
reading frame encoding a mature protein with 32% and 30% identity to
mouse and human CD5 polypeptides, respectively. The molecule consists
of a 330-amino acid extracellular region with three repeats of the
scavenger receptor cysteine-rich domain, a 29-amino acid hydrophobic
transmembrane domain, and a 93-amino acid cytoplasmic tail. The
cytoplasmic region contains motifs that are highly conserved between
species, including several potential phosphorylation sites. The chicken
CD5 is a 64-kDa phosphorylated glycoprotein with a protein core of 57
kDa as determined by immunoprecipitation and SDS-PAGE analysis. 
ß
T cells express a homogeneously high level of CD5, whereas low or
intermediate CD5 expression on 
T cells depends on their tissue
location. In contrast to human and mouse, CD5 is found at low levels on
all chicken B cells. The high conservation of structural features, as
well as signaling motifs, implies a conserved role for CD5 both in
lymphocyte development and function.
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