Cargando…

A secreted metal-binding protein protects necrotrophic phytopathogens from reactive oxygen species

Few secreted proteins involved in plant infection common to necrotrophic bacteria, fungi and oomycetes have been identified except for plant cell wall-degrading enzymes. Here we study a family of iron-binding proteins that is present in Gram-negative and Gram-positive bacteria, fungi, oomycetes and...

Descripción completa

Detalles Bibliográficos
Autores principales: Liu, Lulu, Gueguen-Chaignon, Virginie, Gonçalves, Isabelle R, Rascle, Christine, Rigault, Martine, Dellagi, Alia, Loisel, Elise, Poussereau, Nathalie, Rodrigue, Agnès, Terradot, Laurent, Condemine, Guy
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6813330/
https://www.ncbi.nlm.nih.gov/pubmed/31649262
http://dx.doi.org/10.1038/s41467-019-12826-x
_version_ 1783462816869515264
author Liu, Lulu
Gueguen-Chaignon, Virginie
Gonçalves, Isabelle R
Rascle, Christine
Rigault, Martine
Dellagi, Alia
Loisel, Elise
Poussereau, Nathalie
Rodrigue, Agnès
Terradot, Laurent
Condemine, Guy
author_facet Liu, Lulu
Gueguen-Chaignon, Virginie
Gonçalves, Isabelle R
Rascle, Christine
Rigault, Martine
Dellagi, Alia
Loisel, Elise
Poussereau, Nathalie
Rodrigue, Agnès
Terradot, Laurent
Condemine, Guy
author_sort Liu, Lulu
collection PubMed
description Few secreted proteins involved in plant infection common to necrotrophic bacteria, fungi and oomycetes have been identified except for plant cell wall-degrading enzymes. Here we study a family of iron-binding proteins that is present in Gram-negative and Gram-positive bacteria, fungi, oomycetes and some animals. Homolog proteins in the phytopathogenic bacterium Dickeya dadantii (IbpS) and the fungal necrotroph Botrytis cinerea (BcIbp) are involved in plant infection. IbpS is secreted, can bind iron and copper, and protects the bacteria against H(2)O(2)-induced death. Its 1.7 Å crystal structure reveals a classical Venus Fly trap fold that forms dimers in solution and in the crystal. We propose that secreted Ibp proteins binds exogenous metals and thus limit intracellular metal accumulation and ROS formation in the microorganisms.
format Online
Article
Text
id pubmed-6813330
institution National Center for Biotechnology Information
language English
publishDate 2019
publisher Nature Publishing Group UK
record_format MEDLINE/PubMed
spelling pubmed-68133302019-10-28 A secreted metal-binding protein protects necrotrophic phytopathogens from reactive oxygen species Liu, Lulu Gueguen-Chaignon, Virginie Gonçalves, Isabelle R Rascle, Christine Rigault, Martine Dellagi, Alia Loisel, Elise Poussereau, Nathalie Rodrigue, Agnès Terradot, Laurent Condemine, Guy Nat Commun Article Few secreted proteins involved in plant infection common to necrotrophic bacteria, fungi and oomycetes have been identified except for plant cell wall-degrading enzymes. Here we study a family of iron-binding proteins that is present in Gram-negative and Gram-positive bacteria, fungi, oomycetes and some animals. Homolog proteins in the phytopathogenic bacterium Dickeya dadantii (IbpS) and the fungal necrotroph Botrytis cinerea (BcIbp) are involved in plant infection. IbpS is secreted, can bind iron and copper, and protects the bacteria against H(2)O(2)-induced death. Its 1.7 Å crystal structure reveals a classical Venus Fly trap fold that forms dimers in solution and in the crystal. We propose that secreted Ibp proteins binds exogenous metals and thus limit intracellular metal accumulation and ROS formation in the microorganisms. Nature Publishing Group UK 2019-10-24 /pmc/articles/PMC6813330/ /pubmed/31649262 http://dx.doi.org/10.1038/s41467-019-12826-x Text en © The Author(s) 2019 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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Liu, Lulu
Gueguen-Chaignon, Virginie
Gonçalves, Isabelle R
Rascle, Christine
Rigault, Martine
Dellagi, Alia
Loisel, Elise
Poussereau, Nathalie
Rodrigue, Agnès
Terradot, Laurent
Condemine, Guy
A secreted metal-binding protein protects necrotrophic phytopathogens from reactive oxygen species
title A secreted metal-binding protein protects necrotrophic phytopathogens from reactive oxygen species
title_full A secreted metal-binding protein protects necrotrophic phytopathogens from reactive oxygen species
title_fullStr A secreted metal-binding protein protects necrotrophic phytopathogens from reactive oxygen species
title_full_unstemmed A secreted metal-binding protein protects necrotrophic phytopathogens from reactive oxygen species
title_short A secreted metal-binding protein protects necrotrophic phytopathogens from reactive oxygen species
title_sort secreted metal-binding protein protects necrotrophic phytopathogens from reactive oxygen species
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6813330/
https://www.ncbi.nlm.nih.gov/pubmed/31649262
http://dx.doi.org/10.1038/s41467-019-12826-x
work_keys_str_mv AT liululu asecretedmetalbindingproteinprotectsnecrotrophicphytopathogensfromreactiveoxygenspecies
AT gueguenchaignonvirginie asecretedmetalbindingproteinprotectsnecrotrophicphytopathogensfromreactiveoxygenspecies
AT goncalvesisabeller asecretedmetalbindingproteinprotectsnecrotrophicphytopathogensfromreactiveoxygenspecies
AT rasclechristine asecretedmetalbindingproteinprotectsnecrotrophicphytopathogensfromreactiveoxygenspecies
AT rigaultmartine asecretedmetalbindingproteinprotectsnecrotrophicphytopathogensfromreactiveoxygenspecies
AT dellagialia asecretedmetalbindingproteinprotectsnecrotrophicphytopathogensfromreactiveoxygenspecies
AT loiselelise asecretedmetalbindingproteinprotectsnecrotrophicphytopathogensfromreactiveoxygenspecies
AT poussereaunathalie asecretedmetalbindingproteinprotectsnecrotrophicphytopathogensfromreactiveoxygenspecies
AT rodrigueagnes asecretedmetalbindingproteinprotectsnecrotrophicphytopathogensfromreactiveoxygenspecies
AT terradotlaurent asecretedmetalbindingproteinprotectsnecrotrophicphytopathogensfromreactiveoxygenspecies
AT condemineguy asecretedmetalbindingproteinprotectsnecrotrophicphytopathogensfromreactiveoxygenspecies
AT liululu secretedmetalbindingproteinprotectsnecrotrophicphytopathogensfromreactiveoxygenspecies
AT gueguenchaignonvirginie secretedmetalbindingproteinprotectsnecrotrophicphytopathogensfromreactiveoxygenspecies
AT goncalvesisabeller secretedmetalbindingproteinprotectsnecrotrophicphytopathogensfromreactiveoxygenspecies
AT rasclechristine secretedmetalbindingproteinprotectsnecrotrophicphytopathogensfromreactiveoxygenspecies
AT rigaultmartine secretedmetalbindingproteinprotectsnecrotrophicphytopathogensfromreactiveoxygenspecies
AT dellagialia secretedmetalbindingproteinprotectsnecrotrophicphytopathogensfromreactiveoxygenspecies
AT loiselelise secretedmetalbindingproteinprotectsnecrotrophicphytopathogensfromreactiveoxygenspecies
AT poussereaunathalie secretedmetalbindingproteinprotectsnecrotrophicphytopathogensfromreactiveoxygenspecies
AT rodrigueagnes secretedmetalbindingproteinprotectsnecrotrophicphytopathogensfromreactiveoxygenspecies
AT terradotlaurent secretedmetalbindingproteinprotectsnecrotrophicphytopathogensfromreactiveoxygenspecies
AT condemineguy secretedmetalbindingproteinprotectsnecrotrophicphytopathogensfromreactiveoxygenspecies