Schistosoma mansoni: Structural and biochemical characterization of two distinct Venus Kinase Receptors

[Display omitted] ► Two VKR receptors exist in the parasite Schistosoma mansoni. ► Both receptors are expressed in all parasite stages. ► SmVKR1 and SmVKR2 are potential kinases activated following their binding to distinct ligands. Venus Kinase Receptors (VKRs) are atypical transmembrane proteins c...

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Bibliographic Details
Published in:Experimental parasitology 2012-09, Vol.132 (1), p.32-39
Main Authors: Gouignard, Nadege, Vanderstraete, Mathieu, Cailliau, Katia, Lescuyer, Arlette, Browaeys, Edith, Dissous, Colette
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Biomphalaria
Cloning, Molecular
Cricetinae
Exons
Expression
Female
gene duplication
gene expression
Gene Expression Regulation
genes
Genes, Helminth
gonads
Helminth Proteins - chemistry
Helminth Proteins - genetics
Helminth Proteins - metabolism
insects
insulin receptors
invertebrates
Kinase activity
larvae
Male
Mesocricetus
Molecular Sequence Data
Oocytes - enzymology
Oocytes - metabolism
parasites
parasitology
Phylogeny
Protein-Tyrosine Kinases - metabolism
Receptor Protein-Tyrosine Kinases - chemistry
Receptor Protein-Tyrosine Kinases - genetics
Receptor Protein-Tyrosine Kinases - metabolism
Recombinant proteins
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
reproduction
Schistosoma mansoni
Schistosoma mansoni - enzymology
Schistosoma mansoni - genetics
Schistosoma mansoni - metabolism
Sequence Alignment
Sequence Analysis, Protein
transmembrane proteins
Trematode
tyrosine
Venus Kinase Receptor
Xenopus laevis
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Summary:[Display omitted] ► Two VKR receptors exist in the parasite Schistosoma mansoni. ► Both receptors are expressed in all parasite stages. ► SmVKR1 and SmVKR2 are potential kinases activated following their binding to distinct ligands. 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.
ISSN:0014-4894
1090-2449
DOI:10.1016/j.exppara.2011.05.007