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Abstract: The cytoplasmic tail of mammalian CD8α binds the kinase LCK in a zinc-dependent manner. In analogy with a previous study for humans (Kim et al., 2003) peptides were synthesized from rainbow trout CD8α and LCK. Surface plasmon resonance (SPR) analysis indicated that also in fish these molecules bind to each other in a zinc-dependent manner. [Copyright &y& Elsevier]

Abstract: Partial cDNA sequences of both CD8β and CD4-like (CD4L) genes of common carp (Cyprinus carpio L.) were isolated from thymus cDNA library by the method of suppression subtractive hybridization (SSH). Subsequently the full length cDNAs of carp CD8β and CD4L were obtained by means of 3′ RACE and 5′ RACE, respectively. The full length cDNA of carp CD8β is 1164bp and encodes 207 amino acids including a signal peptide region of 24 amino acids, a transmembrane region of 23 amino acids from aa 167 to aa189 and an immunoglobulin V-set from aa 19 to aa 141. Similar to other species CD8βs, carp CD8β also lacks p56lck domain in the cytoplasmic region. The full length cDNA of carp CD4L is 2001bp and encodes 458 amino acids including four immunoglobulin (Ig)-like domains in the extracellular region, a transmembrane region of 23 amino acids at the C-terminal region from aa 402 to aa 424 and a cytoplasmic tail. Similar to mammalian, avian CD4s and fugu CD4L, carp CD4L also has the conserved p56lck tyrosine kinase motif (C-X-C) in the cytoplasmic region. RT-PCR analysis demonstrated that carp CD8β and CD4L genes were both expressed predominantly in thymus. The results from this study can be used to understand the evolution of both the CD8β and CD4 molecules which can be used as markers for cytotoxic and helper T cells in carp. [Copyright &y& Elsevier]