Novel immunoglobulin-like transcripts in teleost fish encode polymorphic receptors with cytoplasmic ITAM or ITIM an a new structural Ig domain similar to the natural cytotoxicity receptor NKp44

Autor: Jojanneke Jukes, Adrie H. Westphal, Marc Y. Engelsma, Joao Aveiro, Trudi Hermsen, René J. M. Stet, B.M. Lidy Verburg-van Kemenade, J. C. F. M. Dortmans, Huub F. J. Savelkoul
Jazyk: angličtina
Rok vydání: 2005
Předmět:
ID - Infectieziekten
Receptor complex
Carps
Transcription
Genetic
Protein Conformation
Amino Acid Motifs
Molecular Sequence Data
Immunology
carp cyprinus-carpio
Immunoglobulins
Biochemie
Nerve Tissue Proteins
Receptors
Cell Surface
Celbiologie en Immunologie
tumor-cell lysis
Immunoglobulin domain
Biology
Major histocompatibility complex
Biochemistry
Cell Line
functional-characterization
Gene cluster
Genetics
Animals
Gene family
Amino Acid Sequence
Receptors
Immunologic
Databases
Protein
CIDC - Divisie Bacteriologie en TSE's
Receptor
cluster
killer-cells
Polymorphism
Genetic
Base Sequence
Natural Cytotoxicity Triggering Receptor 2
Receptor-Like Protein Tyrosine Phosphatases
Class 2
conservation
histocompatibility complex
zebrafish
Molecular biology
Transmembrane domain
Cell Biology and Immunology
Multigene Family
WIAS
biology.protein
gene family
Immunoglobulin superfamily
member
Protein Tyrosine Phosphatases
Zdroj: Immunogenetics 57 (2005) 1-2
Immunogenetics, 57(1-2), 77-89
ISSN: 0093-7711
Popis: Members of the immunoglobulin superfamily (IgSF) include a group of innate immune receptors located in the leukocyte receptor complex (LRC) and other small clusters such as the TREM/NKp44 cluster. These receptors are characterised by the presence of immunoglobulin domains, a stalk, a transmembrane domain, and a cytoplasmic region containing either an immunoreceptor tyrosine-based inhibitory motif (ITIM) or are linked to an adapter molecule with an activation motif (ITAM) for downstream signalling. We have isolated two carp cDNA sequences encoding receptors in which the extracellular Ig domain structurally resembles the novel V-type Ig domain of NKp44. This is supported by a homology model. The cytoplasmic regions contain either an ITAM (Cyca-NILT1) or ITIMs (Cyca-NILT2). The tissue expression of these receptors is nearly identical, with the highest expression in the immunological organs. Peripheral blood leucocytes showed no detectable expression, but upon in vitro culture expressed NILT1, the activating receptor, and not the inhibitory NILT2 receptor. Southern blot analysis indicated that the NILT1 and NILT2 sequences belong to a multigene family. Analysis of the NILT Ig domain-encoding sequences amplified from both genomic DNA and cDNA revealed extensive haplotypic and allelic polymorphism. Database mining of the zebrafish genome identified several homologs on Chromosome 1, which also contains a cluster of class I major histocompatibility genes. This constellation is reminiscent of the TREM/NKp44 gene cluster and the HLA complex located on human Chromosome 6. The carp NILT genes form a unique cluster of innate immune receptors, which are highly polymorphic, and characterised by a new Ig structural subfamily and are distinct from the novel immune-type receptors (Nitrs) found in other fish species.
Databáze: OpenAIRE
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