Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 405673
Title The superfamily of necrosis and ethylene-inducing peptide 1 (Nep1) like proteins (NLPs) harbors cytotoxic and non-cytotoxic, virulence-promoting members
Author(s) Nuernberger, T.; Kuefner, I.; Anderluh, G.; Oecking, C.; Whisson, S.; Thomma, B.; Ackerveken, G. van den
Source In: Book of Abstracts 26th Fungal Genetics Conference, Asilomar, Pacific Grove, California, USA, 15-20 March 2011. - - p. 50 - 50.
Event 26th Fungal Genetics Conference, Asilomar, Pacific Grove, California, USA, 2011-03-15/2011-03-20
Department(s) Laboratory of Phytopathology
Publication type Abstract in scientific journal or proceedings
Publication year 2011
Abstract Members of the superfamily of necrosis and ethylene-inducing peptide 1 (Nep1) like proteins (NLPs) are widely found in bacteria, fungi and oomycetes. A subset of these proteins causes leaf necrosis on dicot, but not on monocot plants. NLP cytotoxicity was shown to be crucial for microbial virulence and a necrotrophic lifestyle of the producing microbe. X-ray crystallography-based analyses of two microbial NLPs revealed substantial fold conservation of these proteins with cytolytic toxins produced by marine organisms (actinoporins). Actinoporins bind to animal host sphingomyelin prior to membrane pore formation and cytolysis. While plants do not produce sphingomyelins, we show that the target site for NLP toxins is of lipid nature and resides in the outer layer of the plasma membrane of dicot plants. Membrane binding and phytotoxicity requires the presence of a coordinately bound calcium cation within an electrophilic cavity on NLPs, suggesting that the plant docking site is negatively charged. In binding assays, NLPs preferentially bind to phosphorylated phosphatidylinositols (PIP), and incubation of NLPs with PIPs inhibits the cytotoxic activities of these proteins. Thus, NLP susceptibility of plant membranes is determined by its interaction with yet unknown PIP-like lipid structures that define a biologically significant difference in the composition of plasma membranes from monocot and dicot plants. Recently, the production by various oomycetes and fungi of non-cytotoxic members of the NLP superfamily was shown. The possible mode of action of these proteins, their biological activity as well as their contribution to microbial virulence will be discussed
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