Molecular characterization of two vitellogenin genes from the tick, Amblyomma hebraeum (Acari: Ixodidae)
2014
Smith, Alexander D. | Kaufman, W Reuben
We have identified full-length cDNAs encoding two vitellogenins (Vg) from the African bont tick Amblyomma hebraeum Koch (1844). Vg is a large storage protein that is the precursor to vitellin (Vn), the major yolk protein found in eggs. The first Vg cDNA is 5866bp long, with a 5715bp reading frame encoding a 1904 amino acid protein. The second Vg cDNA is 5963bp long, with a 5781 open reading frame encoding a 1926 amino acid protein. Both proteins possess a short N-terminal signal peptide of 21 and 16 amino acids respectively, which following cleavage result in 213.8kDa Vg1 and 215.9kDa Vg2 proteins. The conceptual amino acid translations for both proteins show the N-terminal lipid binding domain, the internal DUF1943 domain and the C-terminal von Willebrand factor type D domain common to all other known Vgs. In addition, these sequences do not resemble any of the conserved sequences that are the hallmarks of the highly similar tick storage protein (carrier protein; CP). Phylogenetic analysis indicates that the Vgs isolated in this study cluster together with other tick Vgs. Using RT-PCR, both Vg1 and Vg2 were expressed only in mated females, and only after they had fed to repletion. In situ hybridizations indicated that both Vgs were expressed only in the midgut and fat body of these females, and was not present in any other female tissues, nor in either fed or unfed males.
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