An odorant-binding protein in the elephant's trunk is finely tuned to sex pheromone (Z)-7-dodecenyl acetate
Abstract Chemical communication in elephants has been well studied at the chemical and behavioural levels. Pheromones have been identified in the Asian elephant (Elephas maximus), including (Z)-7-dodecenyl acetate and frontalin, and their specific effects on the sexual behaviour of elephants have be...
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Nature Portfolio
2022-11-01
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Series: | Scientific Reports |
Online Access: | https://doi.org/10.1038/s41598-022-24214-5 |
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author | Valeriia Zaremska Giovanni Renzone Simona Arena Valentina Ciaravolo Andreas Buberl Folko Balfanz Andrea Scaloni Wolfgang Knoll Paolo Pelosi |
author_facet | Valeriia Zaremska Giovanni Renzone Simona Arena Valentina Ciaravolo Andreas Buberl Folko Balfanz Andrea Scaloni Wolfgang Knoll Paolo Pelosi |
author_sort | Valeriia Zaremska |
collection | DOAJ |
description | Abstract Chemical communication in elephants has been well studied at the chemical and behavioural levels. Pheromones have been identified in the Asian elephant (Elephas maximus), including (Z)-7-dodecenyl acetate and frontalin, and their specific effects on the sexual behaviour of elephants have been accurately documented. In contrast, our knowledge on the proteins mediating detection of pheromones in elephants remains poor and superficial, with only three annotated and reliable entries in sequence databases, two of them being odorant-binding proteins (OBPs), and the third a member of von Ebner's gland (VEG) proteins. Proteomic analysis of trunk wash extract from African elephant (Loxodonta africana) identified one of the OBPs (LafrOBP1) as the main component. We therefore expressed LafrOBP1 and its Asian elephant orthologue in yeast Pichia pastoris and found that both recombinant proteins, as well as the natural LafrOBP1 are tuned to (Z)-7-dodecenyl acetate, but have no affinity for frontalin. Both the natural and recombinant LafrOBP1 carry post-translational modifications such as O-glycosylation, phosphorylation and acetylation, but as these modifications affect only a very small amount of the protein, we cannot establish their potential effects on the ligand-binding properties of OBP1. |
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issn | 2045-2322 |
language | English |
last_indexed | 2024-04-11T13:53:53Z |
publishDate | 2022-11-01 |
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spelling | doaj.art-9017fd1ad11b46f0b2bf3be48d0aa0e02022-12-22T04:20:24ZengNature PortfolioScientific Reports2045-23222022-11-0112111110.1038/s41598-022-24214-5An odorant-binding protein in the elephant's trunk is finely tuned to sex pheromone (Z)-7-dodecenyl acetateValeriia Zaremska0Giovanni Renzone1Simona Arena2Valentina Ciaravolo3Andreas Buberl4Folko Balfanz5Andrea Scaloni6Wolfgang Knoll7Paolo Pelosi8Austrian Institute of Technology GmbH, Biosensor TechnologiesProteomics, Metabolomics and Mass Spectrometry Laboratory, ISPAAM, National Research CouncilProteomics, Metabolomics and Mass Spectrometry Laboratory, ISPAAM, National Research CouncilProteomics, Metabolomics and Mass Spectrometry Laboratory, ISPAAM, National Research CouncilVienna ZooVienna ZooProteomics, Metabolomics and Mass Spectrometry Laboratory, ISPAAM, National Research CouncilAustrian Institute of Technology GmbH, Biosensor TechnologiesAustrian Institute of Technology GmbH, Biosensor TechnologiesAbstract Chemical communication in elephants has been well studied at the chemical and behavioural levels. Pheromones have been identified in the Asian elephant (Elephas maximus), including (Z)-7-dodecenyl acetate and frontalin, and their specific effects on the sexual behaviour of elephants have been accurately documented. In contrast, our knowledge on the proteins mediating detection of pheromones in elephants remains poor and superficial, with only three annotated and reliable entries in sequence databases, two of them being odorant-binding proteins (OBPs), and the third a member of von Ebner's gland (VEG) proteins. Proteomic analysis of trunk wash extract from African elephant (Loxodonta africana) identified one of the OBPs (LafrOBP1) as the main component. We therefore expressed LafrOBP1 and its Asian elephant orthologue in yeast Pichia pastoris and found that both recombinant proteins, as well as the natural LafrOBP1 are tuned to (Z)-7-dodecenyl acetate, but have no affinity for frontalin. Both the natural and recombinant LafrOBP1 carry post-translational modifications such as O-glycosylation, phosphorylation and acetylation, but as these modifications affect only a very small amount of the protein, we cannot establish their potential effects on the ligand-binding properties of OBP1.https://doi.org/10.1038/s41598-022-24214-5 |
spellingShingle | Valeriia Zaremska Giovanni Renzone Simona Arena Valentina Ciaravolo Andreas Buberl Folko Balfanz Andrea Scaloni Wolfgang Knoll Paolo Pelosi An odorant-binding protein in the elephant's trunk is finely tuned to sex pheromone (Z)-7-dodecenyl acetate Scientific Reports |
title | An odorant-binding protein in the elephant's trunk is finely tuned to sex pheromone (Z)-7-dodecenyl acetate |
title_full | An odorant-binding protein in the elephant's trunk is finely tuned to sex pheromone (Z)-7-dodecenyl acetate |
title_fullStr | An odorant-binding protein in the elephant's trunk is finely tuned to sex pheromone (Z)-7-dodecenyl acetate |
title_full_unstemmed | An odorant-binding protein in the elephant's trunk is finely tuned to sex pheromone (Z)-7-dodecenyl acetate |
title_short | An odorant-binding protein in the elephant's trunk is finely tuned to sex pheromone (Z)-7-dodecenyl acetate |
title_sort | odorant binding protein in the elephant s trunk is finely tuned to sex pheromone z 7 dodecenyl acetate |
url | https://doi.org/10.1038/s41598-022-24214-5 |
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