Identification of cell wall-associated proteins from Phytophthora ramorum

H.J.G. Meijer, P.J.I. van de Vondervoort, Q.Y. Yin, C.G. de Koster, F.M. Klis, F. Govers, P.W.J. de Groot

Research output: Contribution to journalArticleAcademicpeer-review

61 Citations (Scopus)

Abstract

The oomycete genus Phytophthora comprises a large group of fungal-like plant pathogens. Two Phytophthora genomes recently have been sequenced; one of them is the genome of Phytophthora ramorum, the causal agent of sudden oak death. During plant infection, extracellular proteins, either soluble secreted proteins or proteins associated with the cell wall, play important roles in the interaction with host plants. Cell walls of P ramorum contain 1 to 1.5% proteins, the remainder almost exclusively being accounted for by glucan polymers. Here, we present an inventory of cell-wall-associated proteins based on mass spectrometric sequence analysis of tryptic peptides obtained by proteolytic digestion of sodium dodecyl sulfate-treated mycelial cell walls. In total, 17 proteins were identified, all of which are authentic secretory proteins. Functional classification based on homology searches revealed six putative mucins or mucin-like proteins, five putative glycoside hydrolases, two transglutaminases, one annexin-like protein, the elicitin protein RAM5, one protein of unknown function, and one Kazal-type protease inhibitor. We propose that the cell wall proteins thus identified are important for pathogenicity.
Original languageEnglish
Pages (from-to)1348-1358
JournalMolecular Plant-Microbe Interactions
Volume19
Issue number12
DOIs
Publication statusPublished - 2006

Keywords

  • acid-sequence similarities
  • thaumatin-like proteins
  • saccharomyces-cerevisiae
  • candida-albicans
  • glycosyl hydrolases
  • extracellular glycoprotein
  • european populations
  • protease inhibitor
  • proteomic analysis
  • molecular-cloning

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