Functional Characteristics of a Novel Chemosensory Protein in the Cotton Bollworm Helicoverpa armigera (Hübner)

A chemosensory protein named HarmCSP5 in cotton bollworm Helicoverpa armigera (Hübner) was obtained from antennal cDNA libraries and expressed in Escherichia coli. The real time quantitative PCR (RT-qPCR) results indicated that HarmCSP5 gene was mainly expressed in male and female antennae but also...

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Main Authors: Tian-tao ZHANG, Wei-xuan WANG, Zi-ding ZHANG, Yong-jun ZHANG, Yu-yuan GUO
Format: Article
Language:English
Published: KeAi Communications Co., Ltd. 2013-05-01
Series:Journal of Integrative Agriculture
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Online Access:http://www.sciencedirect.com/science/article/pii/S2095311913603044
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author Tian-tao ZHANG
Wei-xuan WANG
Zi-ding ZHANG
Yong-jun ZHANG
Yu-yuan GUO
author_facet Tian-tao ZHANG
Wei-xuan WANG
Zi-ding ZHANG
Yong-jun ZHANG
Yu-yuan GUO
author_sort Tian-tao ZHANG
collection DOAJ
description A chemosensory protein named HarmCSP5 in cotton bollworm Helicoverpa armigera (Hübner) was obtained from antennal cDNA libraries and expressed in Escherichia coli. The real time quantitative PCR (RT-qPCR) results indicated that HarmCSP5 gene was mainly expressed in male and female antennae but also expressed in female legs and wings. Competitive binding assays were performed to test the binding affinity of recombinant HarmCSP5 to 60 odor molecules including some cotton volatiles. The resules showed that HarmCSP5 showed strong binding abilities to 4-ehtylbenzaldehyde and 3,4-dimethlbenz aldehyde, whereas methyl phenylacetate, 2-decanone, 1-pentanol, carvenol, isoborneol, nerolidol, 2-nonanone and ethyl heptanoate have relatively weak binding affinity. Moreover, the predicted 3D model of HarmCSP5 consists of six α-helices located among residues 33–38 (α1), 40–48 (α2), 62–72 (α3), 80–96 (α4), 98–108 (α5), and 116–119 (α6), two pairs of disulfide bridges Cys49-Cys55, Cys75-Cys78. The two amino acid residues, Ile94 and Trp101, may play crucial roles in HarmCSP5 binding with ligands and need further study for confirmation.
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spelling doaj-art-477b14acb5f94e09a3d60fb2a577aafb2025-08-02T06:52:13ZengKeAi Communications Co., Ltd.Journal of Integrative Agriculture2095-31192013-05-01125853861Functional Characteristics of a Novel Chemosensory Protein in the Cotton Bollworm Helicoverpa armigera (Hübner)Tian-tao ZHANG0Wei-xuan WANG1Zi-ding ZHANG2Yong-jun ZHANG3Yu-yuan GUO4State Key Laboratory for Biology of Plant Diseases and Insect Pests/Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing 100193, P.R. China; ZHANG Tian-tao, Mobile: 13718631910State Key Laboratory of Agrobiotechnology/College of Biological Sciences, China Agricultural University, Beijing 100193, P.R. ChinaState Key Laboratory of Agrobiotechnology/College of Biological Sciences, China Agricultural University, Beijing 100193, P.R. ChinaState Key Laboratory for Biology of Plant Diseases and Insect Pests/Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing 100193, P.R. China; Correspondence GUO Yu-yuan, Tel/Fax: +86-10-62894786State Key Laboratory for Biology of Plant Diseases and Insect Pests/Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing 100193, P.R. China; ZHANG Yong-jun, Tel: +86-10-62815929A chemosensory protein named HarmCSP5 in cotton bollworm Helicoverpa armigera (Hübner) was obtained from antennal cDNA libraries and expressed in Escherichia coli. The real time quantitative PCR (RT-qPCR) results indicated that HarmCSP5 gene was mainly expressed in male and female antennae but also expressed in female legs and wings. Competitive binding assays were performed to test the binding affinity of recombinant HarmCSP5 to 60 odor molecules including some cotton volatiles. The resules showed that HarmCSP5 showed strong binding abilities to 4-ehtylbenzaldehyde and 3,4-dimethlbenz aldehyde, whereas methyl phenylacetate, 2-decanone, 1-pentanol, carvenol, isoborneol, nerolidol, 2-nonanone and ethyl heptanoate have relatively weak binding affinity. Moreover, the predicted 3D model of HarmCSP5 consists of six α-helices located among residues 33–38 (α1), 40–48 (α2), 62–72 (α3), 80–96 (α4), 98–108 (α5), and 116–119 (α6), two pairs of disulfide bridges Cys49-Cys55, Cys75-Cys78. The two amino acid residues, Ile94 and Trp101, may play crucial roles in HarmCSP5 binding with ligands and need further study for confirmation.http://www.sciencedirect.com/science/article/pii/S2095311913603044Helicoverpa armigerachemosensory proteinexpression characteristicscompetitive binding assay3D structure model
spellingShingle Tian-tao ZHANG
Wei-xuan WANG
Zi-ding ZHANG
Yong-jun ZHANG
Yu-yuan GUO
Functional Characteristics of a Novel Chemosensory Protein in the Cotton Bollworm Helicoverpa armigera (Hübner)
Journal of Integrative Agriculture
Helicoverpa armigera
chemosensory protein
expression characteristics
competitive binding assay
3D structure model
title Functional Characteristics of a Novel Chemosensory Protein in the Cotton Bollworm Helicoverpa armigera (Hübner)
title_full Functional Characteristics of a Novel Chemosensory Protein in the Cotton Bollworm Helicoverpa armigera (Hübner)
title_fullStr Functional Characteristics of a Novel Chemosensory Protein in the Cotton Bollworm Helicoverpa armigera (Hübner)
title_full_unstemmed Functional Characteristics of a Novel Chemosensory Protein in the Cotton Bollworm Helicoverpa armigera (Hübner)
title_short Functional Characteristics of a Novel Chemosensory Protein in the Cotton Bollworm Helicoverpa armigera (Hübner)
title_sort functional characteristics of a novel chemosensory protein in the cotton bollworm helicoverpa armigera hubner
topic Helicoverpa armigera
chemosensory protein
expression characteristics
competitive binding assay
3D structure model
url http://www.sciencedirect.com/science/article/pii/S2095311913603044
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