Staff Publications

Staff Publications

  • external user (warningwarning)
  • Log in as
  • language uk
  • About

    '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.

    We have a manual that explains all the features 

Record number 439485
Title Cladosporium fulvum effector Ecp6 outcompetes host immune receptor for chitin binding through intrachain LysM dimerization
Author(s) Sanchez Vallet, A.; Saleem-Batcha, R.; Kombrink, A.; Hansen, G.; Valkenburg, D.J.; Mesters, J.R.; Thomma, B.P.H.J.
Source In: Book of Abstracts 27th Fungal Genetics Conference, Asilomar, Pacific Grove, California, USA, 12-17 March 2013. - - p. 245 - 245.
Event 27th Fungal Genetics Conference, 2013-03-12/2013-03-17
Department(s) Laboratory of Phytopathology
EPS-2
Publication type Abstract in scientific journal or proceedings
Publication year 2013
Abstract Successful pathogens secrete effector proteins to deregulate host immunity which is triggered upon detection of pathogen-associated molecular patterns (PAMPs). Several fungal pathogens employ LysM effectors, such as Ecp6 from Cladosporium fulvum, to sequester fungal cell wall-derived chitin oligomers which act as PAMP and would otherwise be recognized by host immune receptors and trigger defense responses. The mechanism by which LysM effectors scavenge chitin molecules remained unknown thus far. Based on crystal structure analysis of Ecp6, we reveal a novel mechanism for chitin binding by intrachain LysM dimerization, leading to a binding groove in which chitin is deeply buried in the effector protein. Isothermal titration calorimetry experiments show that the concerted action of two LysM domains mediates a single chitin binding event with ultra-high (pM) affinity.
Comments
There are no comments yet. You can post the first one!
Post a comment
 
Please log in to use this service. Login as Wageningen University & Research user or guest user in upper right hand corner of this page.