
Ferricrocin synthesis in Magnaporthe grisea and its role in pathogenicity in rice
Author(s) -
HOF CAROLIN,
EISFELD KATRIN,
WELZEL KAI,
ANTELO LUIS,
FOSTER ANDREW J.,
ANKE HEIDRUN
Publication year - 2007
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/j.1364-3703.2007.00380.x
Subject(s) - siderophore , magnaporthe grisea , biology , virulence , microbiology and biotechnology , nonribosomal peptide , gene , pathogen , mutant , genome , genetics , oryza sativa , biosynthesis
SUMMARY Iron is an essential element for the growth of nearly all organisms. In order to overcome the problem of its low bioavailability, microorganisms (including fungi) secrete siderophores, high‐affinity iron chelators. As the acquisition of iron is also a key step in infection processes, siderophores have been considered as potential virulence factors in several host–pathogen interactions. Most fungi produce siderophores of the hydroxamate‐type, which are synthesized by non‐ribosomal peptide synthetases (NRPSs). Magnaporthe grisea , the causal agent of rice blast disease, produces ferricrocin as intracellular storage siderophore and excretes coprogens. In the M. grisea genome we identified SSM1 , an NRPS gene, and a gene encoding an l ‐ornithine N5‐monooxygenase ( OMO1 ) that is clustered with SSM1 and responsible for catalysing the first step in siderophore biosynthesis, the N 5 hydroxylation of ornithine. Disruption of SSM1 confirmed that the gene encodes ferricrocin synthetase. Pathogenicity of these mutants towards rice was reduced, suggesting a role of this siderophore in pathogenicity of M. grisea .