Open AccessChaperones of the endoplasmic reticulum are required for Ve1 ‐mediated resistance to V erticillium
Author(s) -
Liebrand Thomas W. H.,
Kombrink Anja,
Zhang Zhao,
Sklenar Jan,
Jones Alexandra M. E.,
Robatzek Silke,
Thomma Bart P. H. J.,
Joosten Matthieu H. A. J.
Publication year - 2014
Publication title -
molecular plant pathology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.945
H-Index - 103
eISSN - 1364-3703
pISSN - 1464-6722
DOI - 10.1111/mpp.12071
Subject(s) - calreticulin , endoplasmic reticulum , biology , microbiology and biotechnology , calnexin
Summary The tomato receptor‐like protein ( RLP ) Ve1 mediates resistance to the vascular fungal pathogen V erticillium dahliae . To identify the proteins required for Ve1 function, we transiently expressed and immunopurified functional Ve1 ‐enhanced green fluorescent protein ( eGFP ) from N icotiana benthamiana leaves, followed by mass spectrometry. This resulted in the identification of peptides originating from the endoplasmic reticulum ( ER )‐resident chaperones HSP70 binding proteins ( BiPs ) and a lectin‐type calreticulin ( CRT ). Knock‐down of the different BiP s and CRT s in tomato resulted in compromised Ve1 ‐mediated resistance to V . dahliae in most cases, showing that these chaperones play an important role in Ve1 functionality. Recently, it has been shown that one particular CRT is required for the biogenesis of the RLP ‐type C ladosporium fulvum resistance protein C f‐4 of tomato, as silencing of CRT3a resulted in a reduced pool of complex glycosylated C f‐4 protein. In contrast, knock‐down of the various CRT s in N . benthamiana or N . tabacum did not result in reduced accumulation of mature complex glycosylated Ve1 protein. Together, this study shows that the BiP and CRT ER chaperones differentially contribute to C f‐4‐ and Ve1 ‐mediated immunity.