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Molecular basis for functional diversity among microbial Nep1-like proteins
Necrosis and ethylene-inducing peptide 1 (Nep1)-like proteins (NLPs) are secreted by several phytopathogenic microorganisms. They trigger necrosis in various eudicot plants upon binding to plant sphingolipid glycosylinositol phosphorylceramides (GIPC). Interestingly, HaNLP3 from the obligate biotrop...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6743777/ https://www.ncbi.nlm.nih.gov/pubmed/31479498 http://dx.doi.org/10.1371/journal.ppat.1007951 |
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author | Lenarčič, Tea Pirc, Katja Hodnik, Vesna Albert, Isabell Borišek, Jure Magistrato, Alessandra Nürnberger, Thorsten Podobnik, Marjetka Anderluh, Gregor |
author_facet | Lenarčič, Tea Pirc, Katja Hodnik, Vesna Albert, Isabell Borišek, Jure Magistrato, Alessandra Nürnberger, Thorsten Podobnik, Marjetka Anderluh, Gregor |
author_sort | Lenarčič, Tea |
collection | PubMed |
description | Necrosis and ethylene-inducing peptide 1 (Nep1)-like proteins (NLPs) are secreted by several phytopathogenic microorganisms. They trigger necrosis in various eudicot plants upon binding to plant sphingolipid glycosylinositol phosphorylceramides (GIPC). Interestingly, HaNLP3 from the obligate biotroph oomycete Hyaloperonospora arabidopsidis does not induce necrosis. We determined the crystal structure of HaNLP3 and showed that it adopts the NLP fold. However, the conformations of the loops surrounding the GIPC headgroup-binding cavity differ from those of cytotoxic Pythium aphanidermatum NLP(Pya). Essential dynamics extracted from μs-long molecular dynamics (MD) simulations reveals a limited conformational plasticity of the GIPC-binding cavity in HaNLP3 relative to toxic NLPs. This likely precludes HaNLP3 binding to GIPCs, which is the underlying reason for the lack of toxicity. This study reveals that mutations at key protein regions cause a switch between non-toxic and toxic phenotypes within the same protein scaffold. Altogether, these data provide evidence that protein flexibility is a distinguishing trait of toxic NLPs and highlight structural determinants for a potential functional diversification of non-toxic NLPs utilized by biotrophic plant pathogens. |
format | Online Article Text |
id | pubmed-6743777 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-67437772019-09-20 Molecular basis for functional diversity among microbial Nep1-like proteins Lenarčič, Tea Pirc, Katja Hodnik, Vesna Albert, Isabell Borišek, Jure Magistrato, Alessandra Nürnberger, Thorsten Podobnik, Marjetka Anderluh, Gregor PLoS Pathog Research Article Necrosis and ethylene-inducing peptide 1 (Nep1)-like proteins (NLPs) are secreted by several phytopathogenic microorganisms. They trigger necrosis in various eudicot plants upon binding to plant sphingolipid glycosylinositol phosphorylceramides (GIPC). Interestingly, HaNLP3 from the obligate biotroph oomycete Hyaloperonospora arabidopsidis does not induce necrosis. We determined the crystal structure of HaNLP3 and showed that it adopts the NLP fold. However, the conformations of the loops surrounding the GIPC headgroup-binding cavity differ from those of cytotoxic Pythium aphanidermatum NLP(Pya). Essential dynamics extracted from μs-long molecular dynamics (MD) simulations reveals a limited conformational plasticity of the GIPC-binding cavity in HaNLP3 relative to toxic NLPs. This likely precludes HaNLP3 binding to GIPCs, which is the underlying reason for the lack of toxicity. This study reveals that mutations at key protein regions cause a switch between non-toxic and toxic phenotypes within the same protein scaffold. Altogether, these data provide evidence that protein flexibility is a distinguishing trait of toxic NLPs and highlight structural determinants for a potential functional diversification of non-toxic NLPs utilized by biotrophic plant pathogens. Public Library of Science 2019-09-03 /pmc/articles/PMC6743777/ /pubmed/31479498 http://dx.doi.org/10.1371/journal.ppat.1007951 Text en © 2019 Lenarčič et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Lenarčič, Tea Pirc, Katja Hodnik, Vesna Albert, Isabell Borišek, Jure Magistrato, Alessandra Nürnberger, Thorsten Podobnik, Marjetka Anderluh, Gregor Molecular basis for functional diversity among microbial Nep1-like proteins |
title | Molecular basis for functional diversity among microbial Nep1-like proteins |
title_full | Molecular basis for functional diversity among microbial Nep1-like proteins |
title_fullStr | Molecular basis for functional diversity among microbial Nep1-like proteins |
title_full_unstemmed | Molecular basis for functional diversity among microbial Nep1-like proteins |
title_short | Molecular basis for functional diversity among microbial Nep1-like proteins |
title_sort | molecular basis for functional diversity among microbial nep1-like proteins |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6743777/ https://www.ncbi.nlm.nih.gov/pubmed/31479498 http://dx.doi.org/10.1371/journal.ppat.1007951 |
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