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Varroa chemosensory proteins: some are conserved across Arthropoda but others are arachnid specific
Author(s) -
Eliash N.,
Thangarajan S.,
Goldenberg I.,
Sela N.,
Kupervaser M.,
Barlev J.,
Altman Y.,
Knyazer A.,
Kamer Y.,
Zaidman I.,
Rafaeli A.,
Soroker V.
Publication year - 2019
Publication title -
insect molecular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.955
H-Index - 93
eISSN - 1365-2583
pISSN - 0962-1075
DOI - 10.1111/imb.12553
Subject(s) - biology , varroa destructor , mite , varroa , transcriptome , adaptation (eye) , genetics , gene , zoology , evolutionary biology , microbiology and biotechnology , gene expression , botany , neuroscience
The tight synchronization between the life cycle of the obligatory parasitic mite Varroa destructor (Varroa) and its host, the honeybee, is mediated by honeybee chemical stimuli. These stimuli are mainly perceived by a pit organ located on the distal part of the mite’s foreleg. In the present study, we searched for Varroa chemosensory molecular components by comparing transcriptomic and proteomic profiles between forelegs from different physiological stages, and rear legs. In general, a comparative transcriptomic analysis showed a clear separation of the expression profiles between the rear legs and the three groups of forelegs (phoretic, reproductive and tray‐collected mites). Most of the differentially expressed transcripts and proteins in the mite’s foreleg were previously uncharacterized. Using a conserved domain approach, we identified 45 transcripts with known chemosensory domains belonging to seven chemosensory protein families, of which 14 were significantly upregulated in the mite’s forelegs when compared to rear legs. These are soluble and membrane bound proteins, including the somewhat ignored receptors of degenerin/epithelial Na+ channels and transient receptor potentials. Phylogenetic clustering and expression profiles of the putative chemosensory proteins suggest their role in chemosensation and shed light on the evolution of these proteins in Chelicerata.