Schistosoma mansoni: Structural and biochemical characterization of two distinct Venus Kinase Receptors
Autor: | Nadège Gouignard, Colette Dissous, Edith Browaeys, Arlette Lescuyer, Katia Cailliau, Mathieu Vanderstraete |
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Rok vydání: | 2012 |
Předmět: |
Male
Molecular Sequence Data Immunology Biology Xenopus laevis Sequence Analysis Protein Cricetinae Gene duplication Animals Amino Acid Sequence Cloning Molecular Kinase activity Gene Genes Helminth Phylogeny Regulation of gene expression Biomphalaria Mesocricetus Receptor Protein-Tyrosine Kinases Exons Helminth Proteins Schistosoma mansoni General Medicine Protein-Tyrosine Kinases biology.organism_classification Recombinant Proteins Transmembrane protein Cell biology Insulin receptor Infectious Diseases Gene Expression Regulation Oocytes biology.protein Female Parasitology Sequence Alignment Tyrosine kinase |
Zdroj: | Experimental Parasitology. 132:32-39 |
ISSN: | 0014-4894 |
DOI: | 10.1016/j.exppara.2011.05.007 |
Popis: | Venus Kinase Receptors (VKRs) are atypical transmembrane proteins composed of an extracellular Venus FlyTrap module linked through a single helix to a tyrosine kinase domain similar to that of insulin receptors. This structure was first described in Schistosoma mansoni, then in a selected range of invertebrates, including many insects. The preferential expression of VKRs in larvae and gonads suggested their role in development and reproduction. While a single vkr gene was consistently found in all genomes, we identified two distinct vkr genes in S. mansoni. Our data indicated that Smvkr1 and Smvkr2 are very similar in structure and likely originated from gene duplication. Both genes are expressed in all the parasite stages and encode homologous proteins with a conserved VKR structure. Recombinant SmVKR1 and SmVKR2 exhibit tyrosine kinase activities dependent on the binding of distinct small ligand molecules. SmVKR1 and SmVKR2 could represent paralogs with different functions in the parasite. |
Databáze: | OpenAIRE |
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