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Título
A highly conserved metalloprotease effector enhances virulence in the maize anthracnose fungus Colletotrichum graminicola
Autor(es)
Materia
Anthracnose
Chitinase
Collectrichum graminicola
Fungalysin
Host-pathogen interaction
Protease
Clasificación UNESCO
2414 Microbiología
2409 Genética
Fecha de publicación
2016
Editor
Molecular Plant Pathology
Citación
Sanz Martín, J.M.; Pacheco Arjona, J.R. [et al.] (2016). A highly conserved metalloprotease effector enhaces virulence in the maize anthracnose fungus Colletotrichum graminicola
Resumen
[EN] Colletotrichum graminicola causes maize anthracnose, an agronomically important disease with a worldwide distribution. We have identified a fungalysin metalloprotease (Cgfl) with a role in virulence. Transcriptional profiling experiments and live cell imaging show that Cgfl is specifically expressed during the biotrophic stage of infection. To determine whether Cgfl has a role in virulence, we obtained null mutants lacking Cgfl and performed pathogenicity and live microscopy assays. The appressorium
morphology of the null mutants is normal, but they exhibit delayed development during the infection process on maize leaves and roots, showing that Cgfl has a role in virulence. In vitro chitinase activity assays of leaves infected with wild-type and null mutant strains show that, in the absence of Cgfl, maize
leaves exhibit increased chitinase activity. Phylogenetic analyses show that Cgfl is highly conserved in fungi. Similarity searches, phylogenetic analysis and transcriptional profiling show that C. graminicola encodes two LysM domain-containing homologues of Ecp6, suggesting that this fungus employs both Cgfl-mediated and LysM protein-mediated strategies to control chitin signalling.
URI
ISSN
1464-6722
DOI
10.1111/mpp.12347
Versión del editor
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