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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KeAi Communications Co., Ltd.
2013-05-01
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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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issn | 2095-3119 |
language | English |
publishDate | 2013-05-01 |
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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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