Utilize este identificador para referenciar este registo: https://hdl.handle.net/10316/108912
Título: Bursaphelenchus xylophilus and B. mucronatus secretomes: a comparative proteomic analysis
Autor: Cardoso, Joana M. S. 
Anjo, Sandra I. 
Fonseca, Luís 
Egas, Conceição 
Manadas, Bruno 
Abrantes, Isabel 
Data: 12-Dez-2016
Projeto: PTDC/AGR-CFL/098916/2008 
PTDC/NEU-NMC/0205/2012 
info:eu-repo/grantAgreement/UID/BIA/04004/2013 
info:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UID/NEU/04539/2013/PT 
REDE/1506/REM/2005 
SFRH/BPD/73724/2010 
SFRH/BD/81495/2011 
SFRH/BPD/101325/2014 
Título da revista, periódico, livro ou evento: Scientific Reports
Volume: 6
Número: 1
Resumo: 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.
URI: https://hdl.handle.net/10316/108912
ISSN: 2045-2322
DOI: 10.1038/srep39007
Direitos: openAccess
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