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A mucin protein predominantly expressed in the female-specific symbiotic organ of the stinkbug Plautia stali

Diverse insects are obligatorily associated with microbial symbionts, wherein the host often develops special symbiotic organs and vertically transmits the symbiont to the next generation. What molecular factors underpin the host-symbiont relationship is of great interest but poorly understood. Here...

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Autores principales: Moriyama, Minoru, Hayashi, Toshinari, Fukatsu, Takema
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9095716/
https://www.ncbi.nlm.nih.gov/pubmed/35546182
http://dx.doi.org/10.1038/s41598-022-11895-1
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author Moriyama, Minoru
Hayashi, Toshinari
Fukatsu, Takema
author_facet Moriyama, Minoru
Hayashi, Toshinari
Fukatsu, Takema
author_sort Moriyama, Minoru
collection PubMed
description Diverse insects are obligatorily associated with microbial symbionts, wherein the host often develops special symbiotic organs and vertically transmits the symbiont to the next generation. What molecular factors underpin the host-symbiont relationship is of great interest but poorly understood. Here we report a novel protein preferentially produced in a female-specific symbiotic organ of the stinkbug Plautia stali, whose posterior midgut develops numerous crypts to host a Pantoea-allied bacterial mutualist. In adult females, several posteriormost crypts are conspicuously enlarged, presumably specialized for vertical symbiont transmission. We detected conspicuous protein bands specific to the female’s swollen crypts by gel electrophoresis, and identified them as representing a novel mucin-like glycoprotein. Histological inspections confirmed that the mucin protein is localized to the female’s swollen crypts, coexisting with a substantial population of the symbiotic bacteria, and excreted from the swollen crypts to the midgut main tract together with the symbiotic bacteria. Using RNA interference, we successfully suppressed production of the mucin protein in adult females of P. stali. However, although the mucin protein was depleted, the symbiont population persisted in the swollen crypts, and vertical symbiont transmission to the next generation occurred. Possible biological roles and evolutionary trajectory of the symbiosis-related mucin protein are discussed.
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spelling pubmed-90957162022-05-13 A mucin protein predominantly expressed in the female-specific symbiotic organ of the stinkbug Plautia stali Moriyama, Minoru Hayashi, Toshinari Fukatsu, Takema Sci Rep Article Diverse insects are obligatorily associated with microbial symbionts, wherein the host often develops special symbiotic organs and vertically transmits the symbiont to the next generation. What molecular factors underpin the host-symbiont relationship is of great interest but poorly understood. Here we report a novel protein preferentially produced in a female-specific symbiotic organ of the stinkbug Plautia stali, whose posterior midgut develops numerous crypts to host a Pantoea-allied bacterial mutualist. In adult females, several posteriormost crypts are conspicuously enlarged, presumably specialized for vertical symbiont transmission. We detected conspicuous protein bands specific to the female’s swollen crypts by gel electrophoresis, and identified them as representing a novel mucin-like glycoprotein. Histological inspections confirmed that the mucin protein is localized to the female’s swollen crypts, coexisting with a substantial population of the symbiotic bacteria, and excreted from the swollen crypts to the midgut main tract together with the symbiotic bacteria. Using RNA interference, we successfully suppressed production of the mucin protein in adult females of P. stali. However, although the mucin protein was depleted, the symbiont population persisted in the swollen crypts, and vertical symbiont transmission to the next generation occurred. Possible biological roles and evolutionary trajectory of the symbiosis-related mucin protein are discussed. Nature Publishing Group UK 2022-05-11 /pmc/articles/PMC9095716/ /pubmed/35546182 http://dx.doi.org/10.1038/s41598-022-11895-1 Text en © The Author(s) 2022 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
Moriyama, Minoru
Hayashi, Toshinari
Fukatsu, Takema
A mucin protein predominantly expressed in the female-specific symbiotic organ of the stinkbug Plautia stali
title A mucin protein predominantly expressed in the female-specific symbiotic organ of the stinkbug Plautia stali
title_full A mucin protein predominantly expressed in the female-specific symbiotic organ of the stinkbug Plautia stali
title_fullStr A mucin protein predominantly expressed in the female-specific symbiotic organ of the stinkbug Plautia stali
title_full_unstemmed A mucin protein predominantly expressed in the female-specific symbiotic organ of the stinkbug Plautia stali
title_short A mucin protein predominantly expressed in the female-specific symbiotic organ of the stinkbug Plautia stali
title_sort mucin protein predominantly expressed in the female-specific symbiotic organ of the stinkbug plautia stali
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9095716/
https://www.ncbi.nlm.nih.gov/pubmed/35546182
http://dx.doi.org/10.1038/s41598-022-11895-1
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