Chemosensory proteins involved in host recognition in the stored-food mite Tyrophagus putrescentiae

BACKGROUND Chemosensory proteins (CSPs) have been proposed to transport a range of aliphatic compounds, esters and other long‐chain compounds. A large number of CSPs from different gene subfamilies have been identified and annotated in arthropods; however, the CSP genes in mites remain unknown. Tyro...

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Published in:Pest management science 2016-08, Vol.72 (8), p.1508-1516
Main Authors: Qu, Shao-Xuan, Ma, Lin, Li, Hui-Ping, Song, Jin-Di, Hong, Xiao-Yue
Format: Article
Language:English
Subjects:
acarid mite
Acaridae - metabolism
Aliphatic compounds
Animals
Anopheles gambiae
Arthropod Proteins - chemistry
Arthropod Proteins - genetics
Arthropod Proteins - metabolism
Arthropoda
Binding Sites
chemosensory proteins
chemosensory recognition
Culex quinquefasciatus
Delia antiqua
Diptera
Drosophila melanogaster
Drosophila simulans
Esters
Female
Insecticides
Ixodes scapularis
Ligands
Male
Mites
Molecular Docking Simulation
olfactory system
Phylogeny
Proteins
Transcriptome
Tyrophagus putrescentiae
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Summary:BACKGROUND Chemosensory proteins (CSPs) have been proposed to transport a range of aliphatic compounds, esters and other long‐chain compounds. A large number of CSPs from different gene subfamilies have been identified and annotated in arthropods; however, the CSP genes in mites remain unknown. Tyrophagus putrescentiae Schrank is an important stored‐product and house‐dust pest. RESULTS By analysing the transcriptome, two putative CSPs were identified, namely TputCSP1 and TputCSP2 (14.9 kDa and 12.1 kDa respectively). The phylogenetic tree showed that the two TputCSPs shared most homology with CSPs in Ixodes scapularis and partially with Diptera, including Anopheles gambiae, Drosophila melanogaster, D. pseudoobscura, D. simulans, Delia antiqua and Culex quinquefasciatus. Additionally, they had similar secondary structure. The 3D models revealed that there are six α‐helices enclosing the hydrophobic ligand binding pocket. Based on a docking study, we found that three ligands, (−)‐alloaromadendrene, 2‐methylnaphthalene and cyclopentadecane, had high binding affinities for TputCSP1. Moreover, the TputCSP2 protein had a higher inhibition constant with different affinities to all test ligands from host volatile substances. CONCLUSION The two CSPs have distinct physiological functions. TputCSP1 may mediate host recognition. © 2015 Society of Chemical Industry
ISSN:1526-498X
1526-4998
DOI:10.1002/ps.4178