The chicken SLAM family

• Published in: Immunogenetics (New York) Vol. 65; no. 1; pp. 63 - 73
• Main Authors: Straub, Christian, Viertlboeck, Birgit C., Göbel, Thomas W.
• Format: Journal Article
• Language: English
• Published: Berlin/Heidelberg Springer-Verlag 2013; Springer Nature B.V
• Subjects: adaptor proteins; Allergology; Amino Acid Sequence; Animals; Antigens, CD - chemistry; Antigens, CD - genetics; Biomedical and Life Sciences; Biomedicine; CD150 antigen; CD48 Antigen; Cell activation; Cell Biology; Chemical bonds; Chickens; Chickens - genetics; Chickens - immunology; Chromosomes; Cloning; Conservation; Cysteine; Disulfide bonds; Gene Function; Genes; Human Genetics; Humans; Immunoglobulins; Immunology; Immunoregulation; Kinases; Leukocytes; Lymphocyte Activation; Lymphocytes; Lymphocytes - immunology; Mammals; Mice; Molecular Sequence Data; Original Paper; Phylogeny; Poultry; Proteins; Receptors, Cell Surface - chemistry; Receptors, Cell Surface - genetics; Receptors, Immunologic - chemistry; Receptors, Immunologic - genetics; SAP protein; Sequence Alignment; Signaling Lymphocytic Activation Molecule Family; Signaling Lymphocytic Activation Molecule Family Member 1; Stress; Xenopus; SLAM family; Chicken; SAP; EAT-2
• ISSN: 0093-7711; 1432-1211
• DOI: 10.1007/s00251-012-0657-6

The signaling lymphocytic activation molecule (SLAM) family of receptors is critically involved in the immune regulation of lymphocytes but has only been detected in mammals, with one member being present in Xenopus . Here, we describe the identification, cloning, and analysis of the chicken homologues to the mammalian SLAMF1 (CD150), SLAMF2 (CD48), and SLAMF4 (CD244, 2B4). Two additional chicken SLAM genes were identified and designated SLAMF3like and SLAM5like in order to stress that those two receptors have no clear mammalian counterpart but share some features with mammalian SLAMF3 and SLAMF5, respectively. Three of the chicken SLAM genes are located on chromosome 25, whereas two are currently not yet assigned. The mammalian and chicken receptors share a common structure with a V-like domain that lacks conserved cysteine residues and a C2-type Ig domain with four cysteines forming two disulfide bonds. Chicken SLAMF2, like its mammalian counterpart, lacks a transmembrane and cytoplasmic domain and thus represents a glycosyl-phosphatidyl-inositol-anchored protein. The cytoplasmic tails of SLAMF1 and SLAMF4 display two and four conserved immunoreceptor tyrosine-based switch motifs (ITSMs), respectively, whereas both chicken SLAMF3like and SLAMF5like have only a single ITSM. We have also identified the chicken homologues of the SLAM-associated protein family of adaptors (SAP), SAP and EAT-2. Chicken SAP shares about 70 % identity with mammalian SAP, and chicken EAT-2 is homologous to mouse EAT-2, whereas human EAT-2 is much shorter. The characterization of the chicken SLAM family of receptors and the SAP adaptors demonstrates the phylogenetic conservation of this family, in particular, its signaling capacities.