Biomolecular NMR Assignments

, Volume 7, Issue 1, pp 109–112 | Cite as

Backbone and sidechain 1H, 13C and 15N chemical shift assignments of the hydrophobin MPG1 from the rice blast fungus Magnaporthe oryzae

  • Anthony A. Rey
  • Antoine Hocher
  • Ann H. Kwan
  • Margaret SundeEmail author


Fungal hydrophobins are secreted proteins that self-assemble at hydrophobic:hydrophilic interfaces. They are essential for a variety of processes in the fungal life cycle, including mediating interactions with surfaces and infection of hosts. The fungus Magnaporthe oryzae, the causative agent of rice blast, relies on the unique properties of hydrophobins to infect cultivated rice as well as over 50 different grass species. The hydrophobin MPG1 is highly expressed during rice blast pathogenesis and has been implicated during host infection. Here we report the backbone and sidechain assignments for the class I hydrophobin MPG1 from the rice blast fungus Magnaporthe oryzae.


Rice blast disease MPG1 Hydrophobin Functional amyloid NMR assignment 



This work was supported by an Australian Research Council Discovery Project (DP0879121). MS was supported by a NHMRC RD Wright Career Development Fellowship.

Conflict of interest

The authors declare that they have no conflict of interest.


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Copyright information

© Springer Science+Business Media B.V. 2012

Authors and Affiliations

  • Anthony A. Rey
    • 1
  • Antoine Hocher
    • 1
  • Ann H. Kwan
    • 1
  • Margaret Sunde
    • 1
    • 2
    Email author
  1. 1.School of Molecular BioscienceUniversity of SydneySydneyAustralia
  2. 2.Discipline of PharmacologyUniversity of SydneySydneyAustralia

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