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...

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Autores principales:	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
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/b32a4e43ff174f97926ad47514d4d920
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spelling	oai:doaj.org-article:b32a4e43ff174f97926ad47514d4d9202021-12-02T17:14:23ZA new non-classical fold of varroa odorant-binding proteins reveals a wide open internal cavity10.1038/s41598-021-92604-22045-2322https://doaj.org/article/b32a4e43ff174f97926ad47514d4d9202021-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-92604-2https://doaj.org/toc/2045-2322Abstract 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.Beatrice AmiguesJiao ZhuAnais GaubertSimona ArenaGiovanni RenzonePhilippe LeoneIsabella Maria FischerHarald PaulsenWolfgang KnollAndrea ScaloniAlain RousselChristian CambillauPaolo PelosiNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-13 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q 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
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.
format	article
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
title	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_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_sort	new non-classical fold of varroa odorant-binding proteins reveals a wide open internal cavity
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/b32a4e43ff174f97926ad47514d4d920
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A new non-classical fold of varroa odorant-binding proteins reveals a wide open internal cavity

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