Molecular and Functional Characterization of Three Odorant-Binding Protein from Periplaneta americana.
The American cockroach, Periplaneta americana, is a vector of many pathogenic organisms associated with human diseases. Olfaction plays a crucial role in guiding cockroach behaviors and contributes to their ability to transmit pathogens. Odorant binding proteins (OBPs), abundant in the insect olfact...
Main Authors: | , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2017-01-01
|
Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC5232348?pdf=render |
_version_ | 1811193665234665472 |
---|---|
author | Zhao-Qun Li Peng He Ya-Nan Zhang Shuang-Lin Dong |
author_facet | Zhao-Qun Li Peng He Ya-Nan Zhang Shuang-Lin Dong |
author_sort | Zhao-Qun Li |
collection | DOAJ |
description | The American cockroach, Periplaneta americana, is a vector of many pathogenic organisms associated with human diseases. Olfaction plays a crucial role in guiding cockroach behaviors and contributes to their ability to transmit pathogens. Odorant binding proteins (OBPs), abundant in the insect olfactory sensilla, are important for insect olfaction. In this study, three OBP genes, PameOBP1, 2 and 3, were cloned from P. americana. Sequence alignment and phylogenetic analysis revealed that PameOBP1, 2 and 3 belong to the Minus-C OBP, Classic OBP, and Plus-C OBP subfamilies, respectively. Expression pattern and ligand-binding analysis showed that PameOBP1 and 2 were specifically expressed in antennae, and exhibited high binding affinities (Ki < 2 μM) to farnesene, farnesol, 2-tridecanone, and tetradecane, suggesting roles in volatile perception. Conversely, PameOBP3 was ubiquitously expressed in most of the tissues examined at high levels and displayed very weak binding affinities (Ki > 40 μM) for all 87 ligands tested. Our study provides insights into the functional diversity of PameOBP genes and provides some volatiles that can potentially be used in behavioral interference of P. americana. |
first_indexed | 2024-04-12T00:13:10Z |
format | Article |
id | doaj.art-d8fb00f84f9f4d3db3cc89367b546d0d |
institution | Directory Open Access Journal |
issn | 1932-6203 |
language | English |
last_indexed | 2024-04-12T00:13:10Z |
publishDate | 2017-01-01 |
publisher | Public Library of Science (PLoS) |
record_format | Article |
series | PLoS ONE |
spelling | doaj.art-d8fb00f84f9f4d3db3cc89367b546d0d2022-12-22T03:55:55ZengPublic Library of Science (PLoS)PLoS ONE1932-62032017-01-01121e017007210.1371/journal.pone.0170072Molecular and Functional Characterization of Three Odorant-Binding Protein from Periplaneta americana.Zhao-Qun LiPeng HeYa-Nan ZhangShuang-Lin DongThe American cockroach, Periplaneta americana, is a vector of many pathogenic organisms associated with human diseases. Olfaction plays a crucial role in guiding cockroach behaviors and contributes to their ability to transmit pathogens. Odorant binding proteins (OBPs), abundant in the insect olfactory sensilla, are important for insect olfaction. In this study, three OBP genes, PameOBP1, 2 and 3, were cloned from P. americana. Sequence alignment and phylogenetic analysis revealed that PameOBP1, 2 and 3 belong to the Minus-C OBP, Classic OBP, and Plus-C OBP subfamilies, respectively. Expression pattern and ligand-binding analysis showed that PameOBP1 and 2 were specifically expressed in antennae, and exhibited high binding affinities (Ki < 2 μM) to farnesene, farnesol, 2-tridecanone, and tetradecane, suggesting roles in volatile perception. Conversely, PameOBP3 was ubiquitously expressed in most of the tissues examined at high levels and displayed very weak binding affinities (Ki > 40 μM) for all 87 ligands tested. Our study provides insights into the functional diversity of PameOBP genes and provides some volatiles that can potentially be used in behavioral interference of P. americana.http://europepmc.org/articles/PMC5232348?pdf=render |
spellingShingle | Zhao-Qun Li Peng He Ya-Nan Zhang Shuang-Lin Dong Molecular and Functional Characterization of Three Odorant-Binding Protein from Periplaneta americana. PLoS ONE |
title | Molecular and Functional Characterization of Three Odorant-Binding Protein from Periplaneta americana. |
title_full | Molecular and Functional Characterization of Three Odorant-Binding Protein from Periplaneta americana. |
title_fullStr | Molecular and Functional Characterization of Three Odorant-Binding Protein from Periplaneta americana. |
title_full_unstemmed | Molecular and Functional Characterization of Three Odorant-Binding Protein from Periplaneta americana. |
title_short | Molecular and Functional Characterization of Three Odorant-Binding Protein from Periplaneta americana. |
title_sort | molecular and functional characterization of three odorant binding protein from periplaneta americana |
url | http://europepmc.org/articles/PMC5232348?pdf=render |
work_keys_str_mv | AT zhaoqunli molecularandfunctionalcharacterizationofthreeodorantbindingproteinfromperiplanetaamericana AT penghe molecularandfunctionalcharacterizationofthreeodorantbindingproteinfromperiplanetaamericana AT yananzhang molecularandfunctionalcharacterizationofthreeodorantbindingproteinfromperiplanetaamericana AT shuanglindong molecularandfunctionalcharacterizationofthreeodorantbindingproteinfromperiplanetaamericana |