Abstract
Insects stimulate specific behaviors by the correct recognition of the chemicals in the external environment. Rhodojaponin III is a botanical grayanoid diterpenid oviposition deterrent isolated from Rhododendron molle. In this study we aimed to determine whether the CSPs involved in the recognition of Rhodojaponin III. A full-length cDNA encoding chemosensory protein was isolated from the antennae of Spodoptera litura Fabricius (CSPSlit, GenBank Accession No. DQ007458). The full-length cDNA of NlFoxA is 1789 bp and has an open reading frame (ORF) of 473 bp, encoding a protein of 126 amino acids, Northern blot analysis revealed that CSPSlit mRNA was mainly expressed in the antennae, legs, wings and female abdomens. A three-dimensional model of CSPSlit was constructed using homology modeling method, and its reliability was evaluated. The active site of CSPSlit was calculated using CDOCKER program indicated that the Tyr24, Ile45, Leu49, Thr64, Leu68, Trp79 and Leu82 were responsible ligand-binding active site on identifying Rhodojaponin III in the CSPSlit. The recombinant CSPSlit protein was expressed in Escherichia coli and purified using single-step Ni-NTA affinity chromatography. Fluorescence emission spectra revealed that the CSPSlit protein had significant affinity to rhodojaponin III. These results mean that CSPSlit is critical for insects identify the Rhodojaponin III.
Highlights
Insects can recognize a variety of plant compounds that stimulate specific behaviors, such as feeding and egg laying by chemoreceptive organs [1,2,3,4]
3.3 3D Modelling of CSPSlit Protein The sequence of CSPSlit was compared to all known proteins in Protein Data Bank (PDB) and the results showed that chemosensory protein A6 from
The CSPSlit was expressed in antennae, legs, wings and female abdomens (Fig.3), these results is similar with the research in other insect [9,21]
Summary
Insects can recognize a variety of plant compounds that stimulate specific behaviors, such as feeding and egg laying (oviposition) by chemoreceptive organs [1,2,3,4]. The CSP was first in Drosophila melanogaster and confirmed that CSPs are capable of binding a range of aliphatic compounds, esters and other long chain compounds that are typical components of pheromonal blends [7,9]. Later studies identified other members of this family in sensory appendages such as antennae, labial palps and legs in a variety of insects [10,11] Several members of this class of protein have been described in insects of different orders, including Lepidoptera [11,12,13,14,15,16,17,18,19], Orthoptera [10,20,21,22], Hymenoptera [7,23,24,25,26], Diptera [27], Blattoidea [28,29], Phasmatodea [30,31,32], Hemiptera [33], etc. Recent studies confirmed that CSPs are capable of binding a range of aliphatic compounds, esters and other long chain compounds that are typical components of pheromonal blends [7,14,15,35]
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
