Journal
BIOCHEMISTRY AND CELL BIOLOGY
Volume 85, Issue 3, Pages 384-394Publisher
CANADIAN SCIENCE PUBLISHING
DOI: 10.1139/O07-051
Keywords
haemaphysalis longicornis tick; valosin containing protein; double-stranded RNA; RNA interference
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We report the cloning and characterization of a cDNA encoding the valosin-containing protein (VCP) from the Haemaphysalis longicornis tick (H1VCP). The full-length H1VCP is 2782 bp and codes for 808 amino acids of a deduced protein with a predicted molecular mass of 89.9 kDa. The domain structure analysis revealed that the deduced protein has 2 Walker A domains, 2 Walker B domains, a Cdc48 domain, and a polyQ-binding domain. The mouse anti-HIVCP serum recognized a 97 kDa native protein in the salivary glands, midgut, and synganglion. RT-PCR analysis revealed that the native VCP was expressed throughout the developing stages and in tick or ans. H1VCP silencing resulted in a decrease in 9 tick body mass after blood feeding. This study not only contributes to a growing understanding of the ATPase gene family but also lays the groundwork for future studies on protein secretion and host-tick interaction. This study is the first report of the VCP gene from Chelicerata, which include spiders, scorpions, and ticks.
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