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  Metabolic priming by a secreted fungal effector

Djamei, A., Schipper, K., Rabe, F., Ghosh, A., Vincon, V., Kahnt, J., et al. (2011). Metabolic priming by a secreted fungal effector. Nature, 478(7369), 395-398. doi:10.1038/nature10454.

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 Creators:
Djamei, A.1, Author           
Schipper, K.1, Author           
Rabe, F.1, Author           
Ghosh, A.2, Author           
Vincon, V.1, Author           
Kahnt, J.3, Author           
Osorio, S., Author
Tohge, T., Author
Fernie, A. R., Author
Feussner, I., Author
Feussner, K., Author
Meinicke, P., Author
Stierhof, Y. D., Author
Schwarz, H., Author
Macek, B., Author
Mann, M., Author
Kahmann, R.4, Author           
Affiliations:
1Department of Organismic Interactions, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266313              
2Max Planck Research Group Molecular Biology of Archaea, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266317              
3Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266280              
4Emeriti Molecular Phytopathology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266291              

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 Abstract: Maize smut caused by the fungus Ustilago maydis is a widespread disease characterized by the development of large plant tumours. U. maydis is a biotrophic pathogen that requires living plant tissue for its development and establishes an intimate interaction zone between fungal hyphae and the plant plasma membrane. U. maydis actively suppresses plant defence responses by secreted protein effectors. Its effector repertoire comprises at least 386 genes mostly encoding proteins of unknown function and expressed exclusively during the biotrophic stage. The U. maydis secretome also contains about 150 proteins with probable roles in fungal nutrition, fungal cell wall modification and host penetration as well as proteins unlikely to act in the fungal-host interface like a chorismate mutase. Chorismate mutases are key enzymes of the shikimate pathway and catalyse the conversion of chorismate to prephenate, the precursor for tyrosine and phenylalanine synthesis. Root-knot nematodes inject a secreted chorismate mutase into plant cells likely to affect development. Here we show that the chorismate mutase Cmu1 secreted by U. maydis is a virulence factor. The enzyme is taken up by plant cells, can spread to neighbouring cells and changes the metabolic status of these cells through metabolic priming. Secreted chorismate mutases are found in many plant-associated microbes and might serve as general tools for host manipulation.

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Language(s): eng - English
 Dates: 2011-10-20
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 583286
ISI: 000296021100048
DOI: 10.1038/nature10454
 Degree: -

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Title: Nature
  Alternative Title : Nature
Source Genre: Journal
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Publ. Info: LONDON : NATURE PUBLISHING GROUP
Pages: - Volume / Issue: 478 (7369) Sequence Number: - Start / End Page: 395 - 398 Identifier: ISSN: 0028-0836