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...
Autores principales: | , , , , , , , , , , |
---|---|
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 |