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Three Amino Acid Residues Bind Corn Odorants to McinOBP1 in the Polyembryonic Endoparasitoid of Macrocentrus cingulum Brischke
Odorant binding proteins (OBPs) play a central role in transporting odorant molecules from the sensillum lymph to olfactory receptors to initiate behavioral responses. In this study, the OBP of Macrocentrus cingulum McinOBP1 was expressed in Escherichia coli and purified by Ni ion affinity chromatog...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3976273/ https://www.ncbi.nlm.nih.gov/pubmed/24705388 http://dx.doi.org/10.1371/journal.pone.0093501 |
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author | Ahmed, Tofael Zhang, Tian-tao Wang, Zhen-ying He, Kang-lai Bai, Shu-xiong |
author_facet | Ahmed, Tofael Zhang, Tian-tao Wang, Zhen-ying He, Kang-lai Bai, Shu-xiong |
author_sort | Ahmed, Tofael |
collection | PubMed |
description | Odorant binding proteins (OBPs) play a central role in transporting odorant molecules from the sensillum lymph to olfactory receptors to initiate behavioral responses. In this study, the OBP of Macrocentrus cingulum McinOBP1 was expressed in Escherichia coli and purified by Ni ion affinity chromatography. Real-time PCR experiments indicate that the McinOBP1 is expressed mainly in adult antennae, with expression levels differing by sex. Ligand-binding experiments using N-phenyl-naphthylamine (1-NPN) as a fluorescent probe demonstrated that the McinOBP1 can bind green-leaf volatiles, including aldehydes and terpenoids, but also can bind aliphatic alcohols with good affinity, in the order trans-2-nonenal>cis-3-hexen-1-ol>trans-caryophelle, suggesting a role of McinOBP1 in general odorant chemoreception. We chose those three odorants for further homology modeling and ligand docking based on their binding affinity. The Val58, Leu62 and Glu130 are the key amino acids in the binding pockets that bind with these three odorants. The three mutants, Val58, Leu62 and Glu130, where the valine, leucine and glutamic residues were replaced by alanine, proline and alanine, respectively; showed reduced affinity to these odorants. This information suggests, Val58, Leu62 and Glu130 are involved in the binding of these compounds, possibly through the specific recognition of ligands that forms hydrogen bonds with the ligands functional groups. |
format | Online Article Text |
id | pubmed-3976273 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-39762732014-04-08 Three Amino Acid Residues Bind Corn Odorants to McinOBP1 in the Polyembryonic Endoparasitoid of Macrocentrus cingulum Brischke Ahmed, Tofael Zhang, Tian-tao Wang, Zhen-ying He, Kang-lai Bai, Shu-xiong PLoS One Research Article Odorant binding proteins (OBPs) play a central role in transporting odorant molecules from the sensillum lymph to olfactory receptors to initiate behavioral responses. In this study, the OBP of Macrocentrus cingulum McinOBP1 was expressed in Escherichia coli and purified by Ni ion affinity chromatography. Real-time PCR experiments indicate that the McinOBP1 is expressed mainly in adult antennae, with expression levels differing by sex. Ligand-binding experiments using N-phenyl-naphthylamine (1-NPN) as a fluorescent probe demonstrated that the McinOBP1 can bind green-leaf volatiles, including aldehydes and terpenoids, but also can bind aliphatic alcohols with good affinity, in the order trans-2-nonenal>cis-3-hexen-1-ol>trans-caryophelle, suggesting a role of McinOBP1 in general odorant chemoreception. We chose those three odorants for further homology modeling and ligand docking based on their binding affinity. The Val58, Leu62 and Glu130 are the key amino acids in the binding pockets that bind with these three odorants. The three mutants, Val58, Leu62 and Glu130, where the valine, leucine and glutamic residues were replaced by alanine, proline and alanine, respectively; showed reduced affinity to these odorants. This information suggests, Val58, Leu62 and Glu130 are involved in the binding of these compounds, possibly through the specific recognition of ligands that forms hydrogen bonds with the ligands functional groups. Public Library of Science 2014-04-04 /pmc/articles/PMC3976273/ /pubmed/24705388 http://dx.doi.org/10.1371/journal.pone.0093501 Text en © 2014 Ahmed et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Ahmed, Tofael Zhang, Tian-tao Wang, Zhen-ying He, Kang-lai Bai, Shu-xiong Three Amino Acid Residues Bind Corn Odorants to McinOBP1 in the Polyembryonic Endoparasitoid of Macrocentrus cingulum Brischke |
title | Three Amino Acid Residues Bind Corn Odorants to McinOBP1 in the Polyembryonic Endoparasitoid of Macrocentrus cingulum Brischke |
title_full | Three Amino Acid Residues Bind Corn Odorants to McinOBP1 in the Polyembryonic Endoparasitoid of Macrocentrus cingulum Brischke |
title_fullStr | Three Amino Acid Residues Bind Corn Odorants to McinOBP1 in the Polyembryonic Endoparasitoid of Macrocentrus cingulum Brischke |
title_full_unstemmed | Three Amino Acid Residues Bind Corn Odorants to McinOBP1 in the Polyembryonic Endoparasitoid of Macrocentrus cingulum Brischke |
title_short | Three Amino Acid Residues Bind Corn Odorants to McinOBP1 in the Polyembryonic Endoparasitoid of Macrocentrus cingulum Brischke |
title_sort | three amino acid residues bind corn odorants to mcinobp1 in the polyembryonic endoparasitoid of macrocentrus cingulum brischke |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3976273/ https://www.ncbi.nlm.nih.gov/pubmed/24705388 http://dx.doi.org/10.1371/journal.pone.0093501 |
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