Molecular cloning and transcriptional and functional analysis of glycogen synthase kinase-3? in Haemaphysalis longicornis (Acari, Ixodidae).
Ontology highlight
ABSTRACT: Glycogen synthase kinase 3 (GSK-3), which belongs to the serine/threonine kinase family, regulates glycogen metabolism, Wnt signaling, hormonal regulation, and embryonic development in many eukaryotes. Here, we cloned a complete open reading frame (ORF) of glycogen synthase kinase 3? (GSK-3?) from Haemaphysalis longicornis and characterized its transcriptional and functional status. The ORF of GSK-3? possesses 1242 nucleotides encoding a mature protein of 413 amino acid residues. GSK-3? nucleotide and protein sequences are highly conserved among different vertebrate and invertebrate animals, with identity between 47.8-100% and 63.2-88.7%, respectively. Sequence comparison showed one signature domain between the residues of 51 and 335 amino acids, which was identified as a protein kinase (serine/threonine). RT-PCR showed GSK-3? mRNA present in all developmental stages of H. longicornis. Interestingly, a higher transcript level was observed in nymph and 7-day-old eggs compared with others by real-time PCR, indicating a role of GSK-3? in the early stages of life. The functional status of GSK-3? was characterized by RNA interference (RNAi) and caused significant (p < 0.05) reduction in feeding and reproduction, as well as an abnormality in eggs and hatching. Taken together, our results suggest that GSK-3? may be an important candidate for a multiple antigen vaccine for controlling the tick population.
SUBMITTER: Rahman MK
PROVIDER: S-EPMC6621911 | biostudies-literature | 2019
REPOSITORIES: biostudies-literature
ACCESS DATA