Bovine WC1 transcripts show evidence of extensive alternative splicing in the extracellular domain [9], suggesting a mechanism to alter bacterial recognition or molecular architecture. The original porcine WC1 cloned is missing one SRCR domain that is present in our sequenced transcripts, and other porcine WC1 transcripts show extensive splicing (manuscript in submission). In contrast, bovine WC1 cytoplasmic tails vary in sequence among genes, but are not alternatively spliced. Ovine and caprine cytoplasmic tails show considerable variation in exon use, but this could be alternative splicing or variation in coding sequence among WC1 genes. The objective here is to test our working hypotheses that (i) the presence or absence of required tyrosines or serines in the WC1 cytoplasmic tail determine whether γδ T cells are activated and WC1 endocytic motifs influence signal duration, and (ii) that splicing out of SRCR domains in the extracellular region affects binding to pathogens.
Janice
Telfer
