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Genomic organization and reproductive regulation of a carrier/storage protein in the Varroa mite, Varroa destructor

A. R. Cabrera, P. D. Shirk, A. J. Duehl, K. V. Donohue, C. M. Grozinger, J. D. Evans, P. E. A. Teal
Insect molecular biology 2013 v.22 no.5 pp. 505-522
fatty acids, RNA interference, ticks, diacylglycerols, phylogeny, Varroa destructor, animal reproduction, males, monoacylglycerols, amino acids, vitellogenin, introns, beta-sitosterol, storage proteins, messenger RNA, heme, transporters, triacylglycerols, mites, cholesterol, cholesteryl esters, sequence homology, Metaseiulus occidentalis
The complete genomic region and corresponding transcript of the most abundant protein in phoretic varroa mites, Varroa destructor (Anderson & Trueman), were sequenced and have homology with acarine hemelipoglycoproteins and the large lipid transfer protein (LLTP) super family. The genomic sequence of VdLLTP included 14 introns and the mature transcript coded for a predicted polypeptide of 1575 amino acid residues. VdLLTP shared a minimum of 25% sequence identity with acarine LLTPs. Phylogenetic assessment showed VdLLTP was most closely related to Metaseiulus occidentalis vitellogenin and LLTP proteins of ticks; however, no heme binding by VdLLTP was detected. Analysis of lipids associated with VdLLTP showed that it was a carrier for free and esterified C12-C22 fatty acids from triglycerides, diacylglycerides and monoacylglycerides. Additionally, cholesterol and β-sitosterol were found as cholesterol esters linked to common fatty acids. Transcript levels of VdLLTP were 42 and 310 times higher in phoretic female mites when compared with males and quiescent deutonymphs, respectively. Coincident with initiation of the reproductive phase, VdLLTP transcript levels declined to a third of those in phoretic female mites. VdLLTP functions as an important lipid transporter and should provide a significant RNA interference target for assessing the control of varroa mites.