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 372020
Title NADPH oxidases are involved in differentiation and pathogenicity in Botrytis cinerea
Author(s) Segmüller, N.; Kokkelink, L.; Giesbert, S.; Odinius, D.; Kan, J. van; Tudzynski, P.
Source Molecular Plant-Microbe Interactions 21 (2008)6. - ISSN 0894-0282 - p. 808 - 819.
DOI https://doi.org/10.1094/MPMI-21-6-0808
Department(s) Laboratory of Phytopathology
EPS-2
Publication type Refereed Article in a scientific journal
Publication year 2008
Keyword(s) respiratory burst oxidase - reactive oxygen - functional-analysis - oxidative burst - active oxygen - cell-growth - disease - localization - infection - virulence
Abstract Nicotinamide adenine dinucleotide (NADPH) oxidases have been shown to be involved in various differentiation processes in fungi. We investigated the role of two NADPH oxidases in the necrotrophic phytopathogenic fungus, Botrytis cinerea. The genes bcnoxA and bcnoxB were cloned and characterized; their deduced amino acid sequences show high homology to fungal NADPH oxidases. Analyses of single and double knock-out mutants of both NADPH oxidase genes showed that both bcnoxA and bcnoxB are involved in formation of sclerotia. Both genes have a great impact on pathogenicity: whereas bcnoxB mutants showed a retarded formation of primary lesions, probably due to an impaired formation of penetration structures, bcnoxA mutants were able to penetrate host tissue in the same way as the wild type but were much slower in colonizing the host tissue. Double mutants showed an additive effect: they were aberrant in penetration and colonization of plant tissue and, therefore, almost nonpathogenic. To study the structure of the fungal Nox complex in more detail, bcnoxR (encoding a homolog of the mammalian p67phox, a regulatory subunit of the Nox complex) was functionally characterized. The phenotype of ¿bcnoxR mutants is identical to that of ¿bcnoxAB double mutants, providing evidence that BcnoxR is involved in activation of both Bcnox enzymes.
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