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Functional evolution of the colony-stimulating factor 1 receptor (CSF1R) and its ligands in birds.
Hume, David A; Gutowska-Ding, Maria W; Garcia-Morales, Carla; Kebede, Adebabay; Bamidele, Oladeji; Trujillo, Adriana Vallejo; Gheyas, Almas A; Smith, Jacqueline.
Afiliación
  • Hume DA; Mater Research Institute-University of Queensland, Translational Research Institute, Woolloongabba, QLD 4102, Australia.
  • Gutowska-Ding MW; The Roslin Institute, University of Edinburgh, Midlothian, United Kingdom.
  • Garcia-Morales C; Department Biotecnologia, Universidad Automona del Estado de Mexico, Toluca Area, Mexico.
  • Kebede A; Department of Microbial, Cellular and Molecular Biology, Addis Ababa University, Addis Ababa, Ethiopia.
  • Bamidele O; Amhara Regional Agricultural Research Institute, Bahir Dar, Ethiopia.
  • Trujillo AV; International Livestock Research Institution (ILRI), Addis Ababa, Ethiopia.
  • Gheyas AA; African Chicken Genetic Gains Project-Nigeria, The International Livestock Research Institute (ILRI), Addis Ababa, Ethiopia.
  • Smith J; Cells, Organisms and Molecular Genetics, School of Life Sciences, University of Nottingham, Nottingham, United Kingdom.
J Leukoc Biol ; 107(2): 237-250, 2020 02.
Artículo en Inglés | MEDLINE | ID: mdl-31487076
ABSTRACT
Macrophage colony-stimulating factor (CSF1 or M-CSF) and interleukin 34 (IL34) are secreted cytokines that control macrophage survival and differentiation. Both act through the CSF1 receptor (CSF1R), a type III transmembrane receptor tyrosine kinase. The functions of CSF1R and both ligands are conserved in birds. We have analyzed protein-coding sequence divergence among avian species. The intracellular tyrosine kinase domain of CSF1R was highly conserved in bird species as in mammals but the extracellular domain of avian CSF1R was more divergent in birds with multiple positively selected amino acids. Based upon crystal structures of the mammalian CSF1/IL34 receptor-ligand interfaces and structure-based alignments, we identified amino acids involved in avian receptor-ligand interactions. The contact amino acids in both CSF1 and CSF1R diverged among avian species. Ligand-binding domain swaps between chicken and zebra finch CSF1 confirmed the function of variants that confer species specificity on the interaction of CSF1 with CSF1R. Based upon genomic sequence analysis, we identified prevalent amino acid changes in the extracellular domain of CSF1R even within the chicken species that distinguished commercial broilers and layers and tropically adapted breeds. The rapid evolution in the extracellular domain of avian CSF1R suggests that at least in birds this ligand-receptor interaction is subjected to pathogen selection. We discuss this finding in the context of expression of CSF1R in antigen-sampling and antigen-presenting cells.
Asunto(s)
Texto completo: Disponible Colección: Bases de datos internacionales Base de datos: MEDLINE Asunto principal: Polimorfismo Genético / Factor Estimulante de Colonias de Macrófagos / Interleucinas / Receptor de Factor Estimulante de Colonias de Macrófagos / Evolución Biológica Límite: Animales Idioma: Inglés Revista: J Leukoc Biol Año: 2020 Tipo del documento: Artículo País de afiliación: Australia

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Texto completo: Disponible Colección: Bases de datos internacionales Base de datos: MEDLINE Asunto principal: Polimorfismo Genético / Factor Estimulante de Colonias de Macrófagos / Interleucinas / Receptor de Factor Estimulante de Colonias de Macrófagos / Evolución Biológica Límite: Animales Idioma: Inglés Revista: J Leukoc Biol Año: 2020 Tipo del documento: Artículo País de afiliación: Australia