Cargando…

Functional Analysis of Two Odorant-Binding Proteins, MaltOBP9 and MaltOBP10, in Monochamus alternatus Hope

Odorant-binding proteins (OBPs) are important for the perception of chemical signals by insects. Effective pest management strategies can be developed by understanding the host location mechanism and the physiological functions of OBPs in olfactory detection. In this study, we cloned two OBPs from M...

Descripción completa

Detalles Bibliográficos
Autores principales: Li, Dong-Zhen, Huang, Xiao-Feng, Yang, Rui-Nan, Chen, Jing-Yuan, Wang, Man-Qun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7174603/
https://www.ncbi.nlm.nih.gov/pubmed/32351402
http://dx.doi.org/10.3389/fphys.2020.00317
_version_ 1783524657437081600
author Li, Dong-Zhen
Huang, Xiao-Feng
Yang, Rui-Nan
Chen, Jing-Yuan
Wang, Man-Qun
author_facet Li, Dong-Zhen
Huang, Xiao-Feng
Yang, Rui-Nan
Chen, Jing-Yuan
Wang, Man-Qun
author_sort Li, Dong-Zhen
collection PubMed
description Odorant-binding proteins (OBPs) are important for the perception of chemical signals by insects. Effective pest management strategies can be developed by understanding the host location mechanism and the physiological functions of OBPs in olfactory detection. In this study, we cloned two OBPs from Monochamus alternatus, where MaltOBP9 was highly expressed in multiple insect tissues and MaltOBP10 was highly expressed in the female antenna according to the results of qRT-PCR. The recombinant proteins were successfully purified in vitro. Immunocytochemistry indicated the high expression of MaltOBP9 and MaltOBP10 in the sensillum lymph of sensilla basiconica, sensilla trichodea, sensilla auricillica, and sensilla chaetica, thereby demonstrating their broad participation in semiochemical detection. Both proteins were localized in the inner cavity of mechanoreceptors and they exhibited broad binding abilities with volatiles from pine bark according to fluorescence competitive binding assays. Due to its broad binding ability and distribution, MaltOBP9 may be involved in various physiological processes as well as olfactory detection. MaltOBP10 appears to play a role in the fundamental olfactory recognition process of female adults according to its broad binding ability. These findings suggest that OBPs may have various physiological functions in insects, thereby providing novel insights into the olfactory receptive mechanism.
format Online
Article
Text
id pubmed-7174603
institution National Center for Biotechnology Information
language English
publishDate 2020
publisher Frontiers Media S.A.
record_format MEDLINE/PubMed
spelling pubmed-71746032020-04-29 Functional Analysis of Two Odorant-Binding Proteins, MaltOBP9 and MaltOBP10, in Monochamus alternatus Hope Li, Dong-Zhen Huang, Xiao-Feng Yang, Rui-Nan Chen, Jing-Yuan Wang, Man-Qun Front Physiol Physiology Odorant-binding proteins (OBPs) are important for the perception of chemical signals by insects. Effective pest management strategies can be developed by understanding the host location mechanism and the physiological functions of OBPs in olfactory detection. In this study, we cloned two OBPs from Monochamus alternatus, where MaltOBP9 was highly expressed in multiple insect tissues and MaltOBP10 was highly expressed in the female antenna according to the results of qRT-PCR. The recombinant proteins were successfully purified in vitro. Immunocytochemistry indicated the high expression of MaltOBP9 and MaltOBP10 in the sensillum lymph of sensilla basiconica, sensilla trichodea, sensilla auricillica, and sensilla chaetica, thereby demonstrating their broad participation in semiochemical detection. Both proteins were localized in the inner cavity of mechanoreceptors and they exhibited broad binding abilities with volatiles from pine bark according to fluorescence competitive binding assays. Due to its broad binding ability and distribution, MaltOBP9 may be involved in various physiological processes as well as olfactory detection. MaltOBP10 appears to play a role in the fundamental olfactory recognition process of female adults according to its broad binding ability. These findings suggest that OBPs may have various physiological functions in insects, thereby providing novel insights into the olfactory receptive mechanism. Frontiers Media S.A. 2020-04-15 /pmc/articles/PMC7174603/ /pubmed/32351402 http://dx.doi.org/10.3389/fphys.2020.00317 Text en Copyright © 2020 Li, Huang, Yang, Chen and Wang. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Physiology
Li, Dong-Zhen
Huang, Xiao-Feng
Yang, Rui-Nan
Chen, Jing-Yuan
Wang, Man-Qun
Functional Analysis of Two Odorant-Binding Proteins, MaltOBP9 and MaltOBP10, in Monochamus alternatus Hope
title Functional Analysis of Two Odorant-Binding Proteins, MaltOBP9 and MaltOBP10, in Monochamus alternatus Hope
title_full Functional Analysis of Two Odorant-Binding Proteins, MaltOBP9 and MaltOBP10, in Monochamus alternatus Hope
title_fullStr Functional Analysis of Two Odorant-Binding Proteins, MaltOBP9 and MaltOBP10, in Monochamus alternatus Hope
title_full_unstemmed Functional Analysis of Two Odorant-Binding Proteins, MaltOBP9 and MaltOBP10, in Monochamus alternatus Hope
title_short Functional Analysis of Two Odorant-Binding Proteins, MaltOBP9 and MaltOBP10, in Monochamus alternatus Hope
title_sort functional analysis of two odorant-binding proteins, maltobp9 and maltobp10, in monochamus alternatus hope
topic Physiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7174603/
https://www.ncbi.nlm.nih.gov/pubmed/32351402
http://dx.doi.org/10.3389/fphys.2020.00317
work_keys_str_mv AT lidongzhen functionalanalysisoftwoodorantbindingproteinsmaltobp9andmaltobp10inmonochamusalternatushope
AT huangxiaofeng functionalanalysisoftwoodorantbindingproteinsmaltobp9andmaltobp10inmonochamusalternatushope
AT yangruinan functionalanalysisoftwoodorantbindingproteinsmaltobp9andmaltobp10inmonochamusalternatushope
AT chenjingyuan functionalanalysisoftwoodorantbindingproteinsmaltobp9andmaltobp10inmonochamusalternatushope
AT wangmanqun functionalanalysisoftwoodorantbindingproteinsmaltobp9andmaltobp10inmonochamusalternatushope