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A Proteomic Investigation of Soluble Olfactory Proteins in Anopheles gambiae

Odorant-binding proteins (OBPs) and chemosensory proteins (CSPs) are small soluble polypeptides that bind semiochemicals in the lymph of insect chemosensilla. In the genome of Anopheles gambiae, 66 genes encode OBPs and 8 encode CSPs. Here we monitored their expression through classical proteomics (...

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Autores principales: Mastrobuoni, Guido, Qiao, Huili, Iovinella, Immacolata, Sagona, Simona, Niccolini, Alberto, Boscaro, Francesca, Caputo, Beniamino, Orejuela, Marta R., Torre, Alessandra della, Kempa, Stefan, Felicioli, Antonio, Pelosi, Paolo, Moneti, Gloriano, Dani, Francesca Romana
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3839933/
https://www.ncbi.nlm.nih.gov/pubmed/24282496
http://dx.doi.org/10.1371/journal.pone.0075162
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author Mastrobuoni, Guido
Qiao, Huili
Iovinella, Immacolata
Sagona, Simona
Niccolini, Alberto
Boscaro, Francesca
Caputo, Beniamino
Orejuela, Marta R.
Torre, Alessandra della
Kempa, Stefan
Felicioli, Antonio
Pelosi, Paolo
Moneti, Gloriano
Dani, Francesca Romana
author_facet Mastrobuoni, Guido
Qiao, Huili
Iovinella, Immacolata
Sagona, Simona
Niccolini, Alberto
Boscaro, Francesca
Caputo, Beniamino
Orejuela, Marta R.
Torre, Alessandra della
Kempa, Stefan
Felicioli, Antonio
Pelosi, Paolo
Moneti, Gloriano
Dani, Francesca Romana
author_sort Mastrobuoni, Guido
collection PubMed
description Odorant-binding proteins (OBPs) and chemosensory proteins (CSPs) are small soluble polypeptides that bind semiochemicals in the lymph of insect chemosensilla. In the genome of Anopheles gambiae, 66 genes encode OBPs and 8 encode CSPs. Here we monitored their expression through classical proteomics (2D gel-MS analysis) and a shotgun approach. The latter method proved much more sensitive and therefore more suitable for tiny biological samples as mosquitoes antennae and eggs. Females express a larger number and higher quantities of OBPs in their antennae than males (24 vs 19). OBP9 is the most abundant in the antennae of both sexes, as well as in larvae, pupae and eggs. Of the 8 CSPs, 4 were detected in antennae, while SAP3 was the only one expressed in larvae. Our proteomic results are in fairly good agreement with data of RNA expression reported in the literature, except for OBP4 and OBP5, that we could not identify in our analysis, nor could we detect in Western Blot experiments. The relatively limited number of soluble olfactory proteins expressed at relatively high levels in mosquitoes makes further studies on the coding of chemical messages at the OBP level more accessible, providing for few specific targets. Identification of such proteins in Anopheles gambiae might facilitate future studies on host finding behavior in this important disease vector.
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spelling pubmed-38399332013-11-26 A Proteomic Investigation of Soluble Olfactory Proteins in Anopheles gambiae Mastrobuoni, Guido Qiao, Huili Iovinella, Immacolata Sagona, Simona Niccolini, Alberto Boscaro, Francesca Caputo, Beniamino Orejuela, Marta R. Torre, Alessandra della Kempa, Stefan Felicioli, Antonio Pelosi, Paolo Moneti, Gloriano Dani, Francesca Romana PLoS One Research Article Odorant-binding proteins (OBPs) and chemosensory proteins (CSPs) are small soluble polypeptides that bind semiochemicals in the lymph of insect chemosensilla. In the genome of Anopheles gambiae, 66 genes encode OBPs and 8 encode CSPs. Here we monitored their expression through classical proteomics (2D gel-MS analysis) and a shotgun approach. The latter method proved much more sensitive and therefore more suitable for tiny biological samples as mosquitoes antennae and eggs. Females express a larger number and higher quantities of OBPs in their antennae than males (24 vs 19). OBP9 is the most abundant in the antennae of both sexes, as well as in larvae, pupae and eggs. Of the 8 CSPs, 4 were detected in antennae, while SAP3 was the only one expressed in larvae. Our proteomic results are in fairly good agreement with data of RNA expression reported in the literature, except for OBP4 and OBP5, that we could not identify in our analysis, nor could we detect in Western Blot experiments. The relatively limited number of soluble olfactory proteins expressed at relatively high levels in mosquitoes makes further studies on the coding of chemical messages at the OBP level more accessible, providing for few specific targets. Identification of such proteins in Anopheles gambiae might facilitate future studies on host finding behavior in this important disease vector. Public Library of Science 2013-11-25 /pmc/articles/PMC3839933/ /pubmed/24282496 http://dx.doi.org/10.1371/journal.pone.0075162 Text en © 2013 Mastrobuoni 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
Mastrobuoni, Guido
Qiao, Huili
Iovinella, Immacolata
Sagona, Simona
Niccolini, Alberto
Boscaro, Francesca
Caputo, Beniamino
Orejuela, Marta R.
Torre, Alessandra della
Kempa, Stefan
Felicioli, Antonio
Pelosi, Paolo
Moneti, Gloriano
Dani, Francesca Romana
A Proteomic Investigation of Soluble Olfactory Proteins in Anopheles gambiae
title A Proteomic Investigation of Soluble Olfactory Proteins in Anopheles gambiae
title_full A Proteomic Investigation of Soluble Olfactory Proteins in Anopheles gambiae
title_fullStr A Proteomic Investigation of Soluble Olfactory Proteins in Anopheles gambiae
title_full_unstemmed A Proteomic Investigation of Soluble Olfactory Proteins in Anopheles gambiae
title_short A Proteomic Investigation of Soluble Olfactory Proteins in Anopheles gambiae
title_sort proteomic investigation of soluble olfactory proteins in anopheles gambiae
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3839933/
https://www.ncbi.nlm.nih.gov/pubmed/24282496
http://dx.doi.org/10.1371/journal.pone.0075162
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