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Interactions between the flavescence dorée phytoplasma and its insect vector indicate lectin-type adhesion mediated by the adhesin VmpA

The flavescence dorée phytoplasma undergoes a propagative cycle in its insect vectors by first interacting with the insect cell surfaces, primarily in the midgut lumen and subsequently in the salivary glands. Adhesion of flavescence dorée phytoplasma to insect cells is mediated by the adhesin VmpA....

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Autores principales: Arricau-Bouvery, Nathalie, Duret, Sybille, Dubrana, Marie-Pierre, Desqué, Delphine, Eveillard, Sandrine, Brocard, Lysiane, Malembic-Maher, Sylvie, Foissac, Xavier
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8160148/
https://www.ncbi.nlm.nih.gov/pubmed/34045641
http://dx.doi.org/10.1038/s41598-021-90809-z
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author Arricau-Bouvery, Nathalie
Duret, Sybille
Dubrana, Marie-Pierre
Desqué, Delphine
Eveillard, Sandrine
Brocard, Lysiane
Malembic-Maher, Sylvie
Foissac, Xavier
author_facet Arricau-Bouvery, Nathalie
Duret, Sybille
Dubrana, Marie-Pierre
Desqué, Delphine
Eveillard, Sandrine
Brocard, Lysiane
Malembic-Maher, Sylvie
Foissac, Xavier
author_sort Arricau-Bouvery, Nathalie
collection PubMed
description The flavescence dorée phytoplasma undergoes a propagative cycle in its insect vectors by first interacting with the insect cell surfaces, primarily in the midgut lumen and subsequently in the salivary glands. Adhesion of flavescence dorée phytoplasma to insect cells is mediated by the adhesin VmpA. We hypothesize that VmpA may have lectin-like activity, similar to several adhesins of bacteria that invade the insect gut. We first demonstrated that the luminal surface of the midgut and the basal surface of the salivary gland cells of the natural vector Scaphoideus titanus and those of the experimental vector Euscelidius variegatus were differentially glycosylated. Using ELISA, inhibition and competitive adhesion assays, and protein overlay assays in the Euva-6 insect cell line, we showed that the protein VmpA binds insect proteins in a lectin-like manner. In conclusion, the results of this study indicate that N-acetylglucosamine and mannose present on the surfaces of the midgut and salivary glands serve as recognition sites for the phytoplasma adhesin VmpA.
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spelling pubmed-81601482021-05-28 Interactions between the flavescence dorée phytoplasma and its insect vector indicate lectin-type adhesion mediated by the adhesin VmpA Arricau-Bouvery, Nathalie Duret, Sybille Dubrana, Marie-Pierre Desqué, Delphine Eveillard, Sandrine Brocard, Lysiane Malembic-Maher, Sylvie Foissac, Xavier Sci Rep Article The flavescence dorée phytoplasma undergoes a propagative cycle in its insect vectors by first interacting with the insect cell surfaces, primarily in the midgut lumen and subsequently in the salivary glands. Adhesion of flavescence dorée phytoplasma to insect cells is mediated by the adhesin VmpA. We hypothesize that VmpA may have lectin-like activity, similar to several adhesins of bacteria that invade the insect gut. We first demonstrated that the luminal surface of the midgut and the basal surface of the salivary gland cells of the natural vector Scaphoideus titanus and those of the experimental vector Euscelidius variegatus were differentially glycosylated. Using ELISA, inhibition and competitive adhesion assays, and protein overlay assays in the Euva-6 insect cell line, we showed that the protein VmpA binds insect proteins in a lectin-like manner. In conclusion, the results of this study indicate that N-acetylglucosamine and mannose present on the surfaces of the midgut and salivary glands serve as recognition sites for the phytoplasma adhesin VmpA. Nature Publishing Group UK 2021-05-27 /pmc/articles/PMC8160148/ /pubmed/34045641 http://dx.doi.org/10.1038/s41598-021-90809-z Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Arricau-Bouvery, Nathalie
Duret, Sybille
Dubrana, Marie-Pierre
Desqué, Delphine
Eveillard, Sandrine
Brocard, Lysiane
Malembic-Maher, Sylvie
Foissac, Xavier
Interactions between the flavescence dorée phytoplasma and its insect vector indicate lectin-type adhesion mediated by the adhesin VmpA
title Interactions between the flavescence dorée phytoplasma and its insect vector indicate lectin-type adhesion mediated by the adhesin VmpA
title_full Interactions between the flavescence dorée phytoplasma and its insect vector indicate lectin-type adhesion mediated by the adhesin VmpA
title_fullStr Interactions between the flavescence dorée phytoplasma and its insect vector indicate lectin-type adhesion mediated by the adhesin VmpA
title_full_unstemmed Interactions between the flavescence dorée phytoplasma and its insect vector indicate lectin-type adhesion mediated by the adhesin VmpA
title_short Interactions between the flavescence dorée phytoplasma and its insect vector indicate lectin-type adhesion mediated by the adhesin VmpA
title_sort interactions between the flavescence dorée phytoplasma and its insect vector indicate lectin-type adhesion mediated by the adhesin vmpa
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8160148/
https://www.ncbi.nlm.nih.gov/pubmed/34045641
http://dx.doi.org/10.1038/s41598-021-90809-z
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