Solution structure of the phytotoxic protein PcF: The first characterized member of the Phytophthora PcF toxin family

Giuseppe Nicastro, Giuseppe Orsomando, Elena Ferrari, Lucia Manconi, Filomena Desario, Adolfo Amici, Alessia Naso, Armando Carpaneto, Thelma A. Pertinhez, Silverio Ruggieri, Alberto Spisni

Research output: Contribution to journalArticle

Abstract

The PcF protein from Phytophthora cactorum is the first member of the "PcF toxin family" from the plant pathogens Phytophthora spp. It is able to induce withering in tomato and strawberry leaves. The lack of sequence similarity with other proteins hampers the identification of the molecular mechanisms responsible for its toxicity. Here, we show that the six cysteines form a disulphide pattern that is exclusive for PcF and essential for the protein withering activity. The NMR solution structure identifies a novel fold among protein effectors: a helix-loop-helix motif. The presence of a negatively charged surface suggests that it might act as a site of electrostatic interaction. Interestingly, a good fold match with Ole e 6, a plant protein with allergenic activity, highlighted the spatial superimposition of a stretch of identical residues. This finding suggests a possible biological activity based on molecular mimicry.

Original languageEnglish
Pages (from-to)1786-1791
Number of pages6
JournalProtein Science
Volume18
Issue number8
DOIs
Publication statusPublished - Aug 2009

Keywords

  • Backbone dynamics
  • Extracellular effector
  • NMR solution structure
  • Oomycete plant pathogen
  • PcF toxin family

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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