A new non-classical fold of varroa odorant-binding proteins reveals a wide open internal cavity
Abstract Odorant-binding proteins (OBPs), as they occur in insects, form a distinct class of proteins that apparently has no closely related representatives in other animals. However, ticks, mites, spiders and millipedes contain genes encoding proteins with sequence similarity to insect OBPs. In thi...
| Main Authors: | , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2021-06-01
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| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-021-92604-2 |
| _version_ | 1818978678497869824 |
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| author | Beatrice Amigues Jiao Zhu Anais Gaubert Simona Arena Giovanni Renzone Philippe Leone Isabella Maria Fischer Harald Paulsen Wolfgang Knoll Andrea Scaloni Alain Roussel Christian Cambillau Paolo Pelosi |
| author_facet | Beatrice Amigues Jiao Zhu Anais Gaubert Simona Arena Giovanni Renzone Philippe Leone Isabella Maria Fischer Harald Paulsen Wolfgang Knoll Andrea Scaloni Alain Roussel Christian Cambillau Paolo Pelosi |
| author_sort | Beatrice Amigues |
| collection | DOAJ |
| description | Abstract Odorant-binding proteins (OBPs), as they occur in insects, form a distinct class of proteins that apparently has no closely related representatives in other animals. However, ticks, mites, spiders and millipedes contain genes encoding proteins with sequence similarity to insect OBPs. In this work, we have explored the structure and function of such non-insect OBPs in the mite Varroa destructor, a major pest of honey bee. Varroa OBPs present six cysteines paired into three disulphide bridges, but with positions in the sequence and connections different from those of their insect counterparts. VdesOBP1 structure was determined in two closely related crystal forms and appears to be a monomer. Its structure assembles five α-helices linked by three disulphide bridges, one of them exhibiting a different connection as compared to their insect counterparts. Comparison with classical OBPs reveals that the second of the six α-helices is lacking in VdesOBP1. Ligand-binding experiments revealed molecules able to bind only specific OBPs with a moderate affinity, suggesting that either optimal ligands have still to be identified, or post-translational modifications present in the native proteins may be essential for modulating binding activity, or else these OBPs might represent a failed attempt in evolution and are not used by the mites. |
| first_indexed | 2024-12-20T16:47:27Z |
| format | Article |
| id | doaj.art-b32a4e43ff174f97926ad47514d4d920 |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-12-20T16:47:27Z |
| publishDate | 2021-06-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-b32a4e43ff174f97926ad47514d4d9202022-12-21T19:32:53ZengNature PortfolioScientific Reports2045-23222021-06-0111111310.1038/s41598-021-92604-2A new non-classical fold of varroa odorant-binding proteins reveals a wide open internal cavityBeatrice Amigues0Jiao Zhu1Anais Gaubert2Simona Arena3Giovanni Renzone4Philippe Leone5Isabella Maria Fischer6Harald Paulsen7Wolfgang Knoll8Andrea Scaloni9Alain Roussel10Christian Cambillau11Paolo Pelosi12Architecture et Fonction des Macromolécules Biologiques (AFMB, UMR 6098), Centre National de la Recherche Scientifique (CNRS), Aix-Marseille Université (AMU)Biosensor Technologies, Austrian Institute of Technology GmbHArchitecture et Fonction des Macromolécules Biologiques (AFMB, UMR 6098), Centre National de la Recherche Scientifique (CNRS), Aix-Marseille Université (AMU)Proteomics and Mass Spectrometry Laboratory, ISPAAM, National Research CouncilProteomics and Mass Spectrometry Laboratory, ISPAAM, National Research CouncilArchitecture et Fonction des Macromolécules Biologiques (AFMB, UMR 6098), Centre National de la Recherche Scientifique (CNRS), Aix-Marseille Université (AMU)Biosensor Technologies, Austrian Institute of Technology GmbHFaculty of Biology, Institute of Molecular Physiology, Johannes Gutenberg-Universität MainzBiosensor Technologies, Austrian Institute of Technology GmbHProteomics and Mass Spectrometry Laboratory, ISPAAM, National Research CouncilArchitecture et Fonction des Macromolécules Biologiques (AFMB, UMR 6098), Centre National de la Recherche Scientifique (CNRS), Aix-Marseille Université (AMU)Architecture et Fonction des Macromolécules Biologiques (AFMB, UMR 6098), Centre National de la Recherche Scientifique (CNRS), Aix-Marseille Université (AMU)Biosensor Technologies, Austrian Institute of Technology GmbHAbstract Odorant-binding proteins (OBPs), as they occur in insects, form a distinct class of proteins that apparently has no closely related representatives in other animals. However, ticks, mites, spiders and millipedes contain genes encoding proteins with sequence similarity to insect OBPs. In this work, we have explored the structure and function of such non-insect OBPs in the mite Varroa destructor, a major pest of honey bee. Varroa OBPs present six cysteines paired into three disulphide bridges, but with positions in the sequence and connections different from those of their insect counterparts. VdesOBP1 structure was determined in two closely related crystal forms and appears to be a monomer. Its structure assembles five α-helices linked by three disulphide bridges, one of them exhibiting a different connection as compared to their insect counterparts. Comparison with classical OBPs reveals that the second of the six α-helices is lacking in VdesOBP1. Ligand-binding experiments revealed molecules able to bind only specific OBPs with a moderate affinity, suggesting that either optimal ligands have still to be identified, or post-translational modifications present in the native proteins may be essential for modulating binding activity, or else these OBPs might represent a failed attempt in evolution and are not used by the mites.https://doi.org/10.1038/s41598-021-92604-2 |
| spellingShingle | Beatrice Amigues Jiao Zhu Anais Gaubert Simona Arena Giovanni Renzone Philippe Leone Isabella Maria Fischer Harald Paulsen Wolfgang Knoll Andrea Scaloni Alain Roussel Christian Cambillau Paolo Pelosi A new non-classical fold of varroa odorant-binding proteins reveals a wide open internal cavity Scientific Reports |
| title | A new non-classical fold of varroa odorant-binding proteins reveals a wide open internal cavity |
| title_full | A new non-classical fold of varroa odorant-binding proteins reveals a wide open internal cavity |
| title_fullStr | A new non-classical fold of varroa odorant-binding proteins reveals a wide open internal cavity |
| title_full_unstemmed | A new non-classical fold of varroa odorant-binding proteins reveals a wide open internal cavity |
| title_short | A new non-classical fold of varroa odorant-binding proteins reveals a wide open internal cavity |
| title_sort | new non classical fold of varroa odorant binding proteins reveals a wide open internal cavity |
| url | https://doi.org/10.1038/s41598-021-92604-2 |
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