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Transcriptome-Based Identification of Highly Similar Odorant-Binding Proteins among Neotropical Stink Bugs and Their Egg Parasitoid

Olfaction plays a fundamental role in insect survival through resource location and intra and interspecific communications. We used RNA-Seq to analyze transcriptomes for odorant-binding proteins (OBPs) from major stink bug pest species in Brazil, Euschistus heros, Chinavia ubica, and Dichelops melac...

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Autores principales: Farias, Luciana R., Schimmelpfeng, Pedro H. C., Togawa, Roberto C., Costa, Marcos M. C., Grynberg, Priscila, Martins, Natália F., Borges, Miguel, Blassioli-Moraes, Maria Carolina, Laumann, Raul A., Báo, Sônia N., Paula, Débora P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4498631/
https://www.ncbi.nlm.nih.gov/pubmed/26161752
http://dx.doi.org/10.1371/journal.pone.0132286
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author Farias, Luciana R.
Schimmelpfeng, Pedro H. C.
Togawa, Roberto C.
Costa, Marcos M. C.
Grynberg, Priscila
Martins, Natália F.
Borges, Miguel
Blassioli-Moraes, Maria Carolina
Laumann, Raul A.
Báo, Sônia N.
Paula, Débora P.
author_facet Farias, Luciana R.
Schimmelpfeng, Pedro H. C.
Togawa, Roberto C.
Costa, Marcos M. C.
Grynberg, Priscila
Martins, Natália F.
Borges, Miguel
Blassioli-Moraes, Maria Carolina
Laumann, Raul A.
Báo, Sônia N.
Paula, Débora P.
author_sort Farias, Luciana R.
collection PubMed
description Olfaction plays a fundamental role in insect survival through resource location and intra and interspecific communications. We used RNA-Seq to analyze transcriptomes for odorant-binding proteins (OBPs) from major stink bug pest species in Brazil, Euschistus heros, Chinavia ubica, and Dichelops melacanthus, and from their egg parasitoid, Telenomus podisi. We identified 23 OBPs in E. heros, 25 OBPs in C. ubica, 9 OBPs in D. melacanthus, and 7 OBPs in T. podisi. The deduced amino acid sequences of the full-length OBPs had low intraspecific similarity, but very high similarity between two pairs of OBPs from E. heros and C. ubica (76.4 and 84.0%) and between two pairs of OBPs from the parasitoid and its preferred host E. heros (82.4 and 88.5%), confirmed by a high similarity of their predicted tertiary structures. The similar pairs of OBPs from E. heros and C. ubica may suggest that they have derived from a common ancestor, and retain the same biological function to bind a ligand perceived or produced in both species. The T. podisi OBPs similar to E. heros were not orthologous to any known hymenopteran OBPs, and may have evolved independently and converged to the host OBPs, providing a possible basis for the host location of T. podisi using E. heros semiochemical cues.
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spelling pubmed-44986312015-07-17 Transcriptome-Based Identification of Highly Similar Odorant-Binding Proteins among Neotropical Stink Bugs and Their Egg Parasitoid Farias, Luciana R. Schimmelpfeng, Pedro H. C. Togawa, Roberto C. Costa, Marcos M. C. Grynberg, Priscila Martins, Natália F. Borges, Miguel Blassioli-Moraes, Maria Carolina Laumann, Raul A. Báo, Sônia N. Paula, Débora P. PLoS One Research Article Olfaction plays a fundamental role in insect survival through resource location and intra and interspecific communications. We used RNA-Seq to analyze transcriptomes for odorant-binding proteins (OBPs) from major stink bug pest species in Brazil, Euschistus heros, Chinavia ubica, and Dichelops melacanthus, and from their egg parasitoid, Telenomus podisi. We identified 23 OBPs in E. heros, 25 OBPs in C. ubica, 9 OBPs in D. melacanthus, and 7 OBPs in T. podisi. The deduced amino acid sequences of the full-length OBPs had low intraspecific similarity, but very high similarity between two pairs of OBPs from E. heros and C. ubica (76.4 and 84.0%) and between two pairs of OBPs from the parasitoid and its preferred host E. heros (82.4 and 88.5%), confirmed by a high similarity of their predicted tertiary structures. The similar pairs of OBPs from E. heros and C. ubica may suggest that they have derived from a common ancestor, and retain the same biological function to bind a ligand perceived or produced in both species. The T. podisi OBPs similar to E. heros were not orthologous to any known hymenopteran OBPs, and may have evolved independently and converged to the host OBPs, providing a possible basis for the host location of T. podisi using E. heros semiochemical cues. Public Library of Science 2015-07-10 /pmc/articles/PMC4498631/ /pubmed/26161752 http://dx.doi.org/10.1371/journal.pone.0132286 Text en © 2015 Farias 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
Farias, Luciana R.
Schimmelpfeng, Pedro H. C.
Togawa, Roberto C.
Costa, Marcos M. C.
Grynberg, Priscila
Martins, Natália F.
Borges, Miguel
Blassioli-Moraes, Maria Carolina
Laumann, Raul A.
Báo, Sônia N.
Paula, Débora P.
Transcriptome-Based Identification of Highly Similar Odorant-Binding Proteins among Neotropical Stink Bugs and Their Egg Parasitoid
title Transcriptome-Based Identification of Highly Similar Odorant-Binding Proteins among Neotropical Stink Bugs and Their Egg Parasitoid
title_full Transcriptome-Based Identification of Highly Similar Odorant-Binding Proteins among Neotropical Stink Bugs and Their Egg Parasitoid
title_fullStr Transcriptome-Based Identification of Highly Similar Odorant-Binding Proteins among Neotropical Stink Bugs and Their Egg Parasitoid
title_full_unstemmed Transcriptome-Based Identification of Highly Similar Odorant-Binding Proteins among Neotropical Stink Bugs and Their Egg Parasitoid
title_short Transcriptome-Based Identification of Highly Similar Odorant-Binding Proteins among Neotropical Stink Bugs and Their Egg Parasitoid
title_sort transcriptome-based identification of highly similar odorant-binding proteins among neotropical stink bugs and their egg parasitoid
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4498631/
https://www.ncbi.nlm.nih.gov/pubmed/26161752
http://dx.doi.org/10.1371/journal.pone.0132286
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