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The plant apoplasm is an important recipient compartment for nematode secreted proteins
Similarly to microbial pathogens, plant-parasitic nematodes secrete into their host plants proteins that are essential to establish a functional interaction. Identifying the destination of nematode secreted proteins within plant cell compartment(s) will provide compelling clues on their molecular fu...
Autores principales: | , , , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3022405/ https://www.ncbi.nlm.nih.gov/pubmed/21115667 http://dx.doi.org/10.1093/jxb/erq352 |
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author | Vieira, Paulo Danchin, Etienne G. J. Neveu, Cédric Crozat, Carine Jaubert, Stéphanie Hussey, Richard S. Engler, Gilbert Abad, Pierre de Almeida-Engler, Janice Castagnone-Sereno, Philippe Rosso, Marie-Noëlle |
author_facet | Vieira, Paulo Danchin, Etienne G. J. Neveu, Cédric Crozat, Carine Jaubert, Stéphanie Hussey, Richard S. Engler, Gilbert Abad, Pierre de Almeida-Engler, Janice Castagnone-Sereno, Philippe Rosso, Marie-Noëlle |
author_sort | Vieira, Paulo |
collection | PubMed |
description | Similarly to microbial pathogens, plant-parasitic nematodes secrete into their host plants proteins that are essential to establish a functional interaction. Identifying the destination of nematode secreted proteins within plant cell compartment(s) will provide compelling clues on their molecular functions. Here the fine localization of five nematode secreted proteins was analysed throughout parasitism in Arabidopsis thaliana. An immunocytochemical method was developed that preserves both the host and the pathogen tissues, allowing the localization of nematode secreted proteins within both organisms. One secreted protein from the amphids and three secreted proteins from the subventral oesophageal glands involved in protein degradation and cell wall modification were secreted in the apoplasm during intercellular migration and to a lower extent by early sedentary stages during giant cell formation. Conversely, another protein produced by both subventral and dorsal oesophageal glands in parasitic stages accumulated profusely at the cell wall of young and mature giant cells. In addition, secretion of cell wall-modifying proteins by the vulva of adult females suggested a role in egg laying. The study shows that the plant apoplasm acts as an important destination compartment for proteins secreted during migration and during sedentary stages of the nematode. |
format | Text |
id | pubmed-3022405 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-30224052011-01-18 The plant apoplasm is an important recipient compartment for nematode secreted proteins Vieira, Paulo Danchin, Etienne G. J. Neveu, Cédric Crozat, Carine Jaubert, Stéphanie Hussey, Richard S. Engler, Gilbert Abad, Pierre de Almeida-Engler, Janice Castagnone-Sereno, Philippe Rosso, Marie-Noëlle J Exp Bot Research Papers Similarly to microbial pathogens, plant-parasitic nematodes secrete into their host plants proteins that are essential to establish a functional interaction. Identifying the destination of nematode secreted proteins within plant cell compartment(s) will provide compelling clues on their molecular functions. Here the fine localization of five nematode secreted proteins was analysed throughout parasitism in Arabidopsis thaliana. An immunocytochemical method was developed that preserves both the host and the pathogen tissues, allowing the localization of nematode secreted proteins within both organisms. One secreted protein from the amphids and three secreted proteins from the subventral oesophageal glands involved in protein degradation and cell wall modification were secreted in the apoplasm during intercellular migration and to a lower extent by early sedentary stages during giant cell formation. Conversely, another protein produced by both subventral and dorsal oesophageal glands in parasitic stages accumulated profusely at the cell wall of young and mature giant cells. In addition, secretion of cell wall-modifying proteins by the vulva of adult females suggested a role in egg laying. The study shows that the plant apoplasm acts as an important destination compartment for proteins secreted during migration and during sedentary stages of the nematode. Oxford University Press 2011-01 2010-11-29 /pmc/articles/PMC3022405/ /pubmed/21115667 http://dx.doi.org/10.1093/jxb/erq352 Text en © 2010 The Author(s). This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. This paper is available online free of all access charges (see http://jxb.oxfordjournals.org/open_access.html for further details) |
spellingShingle | Research Papers Vieira, Paulo Danchin, Etienne G. J. Neveu, Cédric Crozat, Carine Jaubert, Stéphanie Hussey, Richard S. Engler, Gilbert Abad, Pierre de Almeida-Engler, Janice Castagnone-Sereno, Philippe Rosso, Marie-Noëlle The plant apoplasm is an important recipient compartment for nematode secreted proteins |
title | The plant apoplasm is an important recipient compartment for nematode secreted proteins |
title_full | The plant apoplasm is an important recipient compartment for nematode secreted proteins |
title_fullStr | The plant apoplasm is an important recipient compartment for nematode secreted proteins |
title_full_unstemmed | The plant apoplasm is an important recipient compartment for nematode secreted proteins |
title_short | The plant apoplasm is an important recipient compartment for nematode secreted proteins |
title_sort | plant apoplasm is an important recipient compartment for nematode secreted proteins |
topic | Research Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3022405/ https://www.ncbi.nlm.nih.gov/pubmed/21115667 http://dx.doi.org/10.1093/jxb/erq352 |
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