Cargando…

Bursaphelenchus xylophilus and B. mucronatus secretomes: a comparative proteomic analysis

The pinewood nematode, Bursaphelenchus xylophilus, recognized as a worldwide major forest pest, is a migratory endoparasitic nematode with capacity to feed on pine tissues and also on fungi colonizing the trees. Bursaphelenchus mucronatus, the closest related species, differs from B. xylophilus on i...

Descripción completa

Detalles Bibliográficos
Autores principales: Cardoso, Joana M. S., Anjo, Sandra I., Fonseca, Luís, Egas, Conceição, Manadas, Bruno, Abrantes, Isabel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5150578/
https://www.ncbi.nlm.nih.gov/pubmed/27941947
http://dx.doi.org/10.1038/srep39007
_version_ 1782474228276133888
author Cardoso, Joana M. S.
Anjo, Sandra I.
Fonseca, Luís
Egas, Conceição
Manadas, Bruno
Abrantes, Isabel
author_facet Cardoso, Joana M. S.
Anjo, Sandra I.
Fonseca, Luís
Egas, Conceição
Manadas, Bruno
Abrantes, Isabel
author_sort Cardoso, Joana M. S.
collection PubMed
description The pinewood nematode, Bursaphelenchus xylophilus, recognized as a worldwide major forest pest, is a migratory endoparasitic nematode with capacity to feed on pine tissues and also on fungi colonizing the trees. Bursaphelenchus mucronatus, the closest related species, differs from B. xylophilus on its pathogenicity, making this nematode a good candidate for comparative analyses. Secretome profiles of B. xylophilus and B. mucronatus were obtained and proteomic differences were evaluated by quantitative SWATH-MS. From the 681 proteins initially identified, 422 were quantified and compared between B. xylophilus and B. mucronatus secretomes and from these, 243 proteins were found differentially regulated: 158 and 85 proteins were increased in B. xylophilus and B. mucronatus secretomes, respectively. While increased proteins in B. xylophilus secretome revealed a strong enrichment in proteins with peptidase activity, the increased proteins in B. mucronatus secretome were mainly related to oxidative stress responses. The changes in peptidases were evaluated at the transcription level by RT-qPCR, revealing a correlation between the mRNA levels of four cysteine peptidases with secretion levels. The analysis presented expands our knowledge about molecular basis of B. xylophilus and B. mucronatus hosts interaction and supports the hypothesis of a key role of secreted peptidases in B. xylophilus pathogenicity.
format Online
Article
Text
id pubmed-5150578
institution National Center for Biotechnology Information
language English
publishDate 2016
publisher Nature Publishing Group
record_format MEDLINE/PubMed
spelling pubmed-51505782016-12-19 Bursaphelenchus xylophilus and B. mucronatus secretomes: a comparative proteomic analysis Cardoso, Joana M. S. Anjo, Sandra I. Fonseca, Luís Egas, Conceição Manadas, Bruno Abrantes, Isabel Sci Rep Article The pinewood nematode, Bursaphelenchus xylophilus, recognized as a worldwide major forest pest, is a migratory endoparasitic nematode with capacity to feed on pine tissues and also on fungi colonizing the trees. Bursaphelenchus mucronatus, the closest related species, differs from B. xylophilus on its pathogenicity, making this nematode a good candidate for comparative analyses. Secretome profiles of B. xylophilus and B. mucronatus were obtained and proteomic differences were evaluated by quantitative SWATH-MS. From the 681 proteins initially identified, 422 were quantified and compared between B. xylophilus and B. mucronatus secretomes and from these, 243 proteins were found differentially regulated: 158 and 85 proteins were increased in B. xylophilus and B. mucronatus secretomes, respectively. While increased proteins in B. xylophilus secretome revealed a strong enrichment in proteins with peptidase activity, the increased proteins in B. mucronatus secretome were mainly related to oxidative stress responses. The changes in peptidases were evaluated at the transcription level by RT-qPCR, revealing a correlation between the mRNA levels of four cysteine peptidases with secretion levels. The analysis presented expands our knowledge about molecular basis of B. xylophilus and B. mucronatus hosts interaction and supports the hypothesis of a key role of secreted peptidases in B. xylophilus pathogenicity. Nature Publishing Group 2016-12-12 /pmc/articles/PMC5150578/ /pubmed/27941947 http://dx.doi.org/10.1038/srep39007 Text en Copyright © 2016, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Cardoso, Joana M. S.
Anjo, Sandra I.
Fonseca, Luís
Egas, Conceição
Manadas, Bruno
Abrantes, Isabel
Bursaphelenchus xylophilus and B. mucronatus secretomes: a comparative proteomic analysis
title Bursaphelenchus xylophilus and B. mucronatus secretomes: a comparative proteomic analysis
title_full Bursaphelenchus xylophilus and B. mucronatus secretomes: a comparative proteomic analysis
title_fullStr Bursaphelenchus xylophilus and B. mucronatus secretomes: a comparative proteomic analysis
title_full_unstemmed Bursaphelenchus xylophilus and B. mucronatus secretomes: a comparative proteomic analysis
title_short Bursaphelenchus xylophilus and B. mucronatus secretomes: a comparative proteomic analysis
title_sort bursaphelenchus xylophilus and b. mucronatus secretomes: a comparative proteomic analysis
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5150578/
https://www.ncbi.nlm.nih.gov/pubmed/27941947
http://dx.doi.org/10.1038/srep39007
work_keys_str_mv AT cardosojoanams bursaphelenchusxylophilusandbmucronatussecretomesacomparativeproteomicanalysis
AT anjosandrai bursaphelenchusxylophilusandbmucronatussecretomesacomparativeproteomicanalysis
AT fonsecaluis bursaphelenchusxylophilusandbmucronatussecretomesacomparativeproteomicanalysis
AT egasconceicao bursaphelenchusxylophilusandbmucronatussecretomesacomparativeproteomicanalysis
AT manadasbruno bursaphelenchusxylophilusandbmucronatussecretomesacomparativeproteomicanalysis
AT abrantesisabel bursaphelenchusxylophilusandbmucronatussecretomesacomparativeproteomicanalysis