TY - JOUR
T1 - Characterization of MaltOBP1, a Minus-C Odorant-Binding Protein, From the Japanese Pine Sawyer Beetle, Monochamus alternatus Hope (Coleoptera: Cerambycidae)
AU - Zhang, Fangmei
AU - Merchant, Austin
AU - Zhao, Zhibin
AU - Zhang, Yunhui
AU - Zhang, Jing
AU - Zhang, Qingwen
AU - Wang, Qinghua
AU - Zhou, Xuguo
AU - Li, Xiangrui
N1 - The authors are grateful for the constructive criticism and comments provided by the reviewers and editor to improve this manuscript. Special thanks go to Drs. Yang Liu and Bing Wang (IPP, CAAS) for their suggestions on an earlier draft. Funding. This research was supported by a Special Fund for Forest Scientific Research in the Public Welfare (Grant No. 201504302), a Capacity Building for International Cooperation in Scientific and Technological Innovation (Grant No. CAFYBB2018GB001), the Project of Science and Technology Innovation Team (Grant No. KJCXTD-201903), Xinyang Agriculture and Forestry University, P.R. China, and a Start-up Fund at the University of Kentucky. The funders had no role in the design of the study; in the collection, analyses, or interpretation of data; in the writing of the manuscript; or in the decision to publish the results.
PY - 2020/4/1
Y1 - 2020/4/1
N2 - Insect Odorant-Binding Proteins (OBPs) play crucial roles in the discrimination, binding and transportation of odorants. Herein, the full-length cDNA sequence of Minus-C OBP1 (MaltOBP1) from the Japanese pine sawyer beetle, Monochamus alternatus, was cloned by 3′ and 5′ RACE-PCR and analyzed. The results showed that MaltOBP1 contains a 435 bp open reading frame (ORF) that encodes 144 amino acids, including a 21-amino acid signal peptide at the N-terminus. The matured MaltOBP1 protein possesses a predicted molecular weight of about 14 kDa and consists of six α-helices, creating an open binding pocket, and two disulfide bridges. Immunoblotting results showed that MaltOBP1 was most highly expressed in antennae in both sexes, followed by wings and legs. Fluorescence assays demonstrated that MaltOBP1 protein exhibited high binding affinity with (R)-(+)-α-pinene, (−)-β-pinene, trans-caryophyllene, (R)-(+)-limonene and (–)-verbenone, which are the main volatile compounds of the pine tree. Our combined results suggest that MaltOBP1 plays a role in host seeking behavior in M. alternatus.
AB - Insect Odorant-Binding Proteins (OBPs) play crucial roles in the discrimination, binding and transportation of odorants. Herein, the full-length cDNA sequence of Minus-C OBP1 (MaltOBP1) from the Japanese pine sawyer beetle, Monochamus alternatus, was cloned by 3′ and 5′ RACE-PCR and analyzed. The results showed that MaltOBP1 contains a 435 bp open reading frame (ORF) that encodes 144 amino acids, including a 21-amino acid signal peptide at the N-terminus. The matured MaltOBP1 protein possesses a predicted molecular weight of about 14 kDa and consists of six α-helices, creating an open binding pocket, and two disulfide bridges. Immunoblotting results showed that MaltOBP1 was most highly expressed in antennae in both sexes, followed by wings and legs. Fluorescence assays demonstrated that MaltOBP1 protein exhibited high binding affinity with (R)-(+)-α-pinene, (−)-β-pinene, trans-caryophyllene, (R)-(+)-limonene and (–)-verbenone, which are the main volatile compounds of the pine tree. Our combined results suggest that MaltOBP1 plays a role in host seeking behavior in M. alternatus.
KW - fluorescence binding assay
KW - Monochamus alternatus
KW - odorant binding protein
KW - olfactory
KW - plant volatile
UR - https://www.scopus.com/pages/publications/85083483158
UR - https://www.scopus.com/pages/publications/85083483158#tab=citedBy
U2 - 10.3389/fphys.2020.00212
DO - 10.3389/fphys.2020.00212
M3 - Article
AN - SCOPUS:85083483158
SN - 1664-042X
VL - 11
JO - Frontiers in Physiology
JF - Frontiers in Physiology
M1 - 212
ER -