Journal of Plant Pathology

, Volume 101, Issue 4, pp 1183–1186 | Cite as

Defensin AFP1 inhibits appressorium formation and penetration of rice cells by the rice blast fungus Magnaporthe oryzae

  • Yoshiyuki SagehashiEmail author
  • Taketo Ashizawa
  • Hiroaki Takaku
  • Osamu Yatou
Short Communication


The plant defensin antifungal peptide 1 (AFP1) is composed of only 51 amino acids and has potent antifungal activity against the rice blast fungus Magnaporthe oryzae. To elucidate the antifungal mechanisms of AFP1, we assessed the suppression of appressorium formation and hyphal penetration by M. oryzae. AFP1 interfered with appressorium formation and host cell penetration following to invasion in a dose-dependent manner. This is the first report of the prevention of M. oryzae infection in rice by AFP1 and our observations could help to develop resistant cultivars and antifungal formulations for use in agriculture.


Defensin Antifungal peptide Magnaporthe oryzae Appressorium formation 



We thank Ms. Yumi Ikeda for her technical support in various experiments; Dr. Takayuki Mitsunaga for support with statistical analysis; Dr. Marie Nishimura for kindly providing the M. oryzae strain. M. oryzae Guy11 was used with the special permission of the Ministry of Agriculture, Forestry and Fisheries of Japan.

Compliance with ethical standards

This article does not contain any studies with human participants or animal performed by any of the authors.

Conflict of interest

The authors declare no conflict of interest.


  1. Cools TL, Struyfs C, Cammue BP, Thevissen K (2017) Antifungal plant defensins: increased insight in their mode of action as a basis for their use to combat fungal infections. Future Microbiol 12:441–454CrossRefGoogle Scholar
  2. De Coninck B, Cammue BP, Thevissen K (2013) Modes of antifungal action and in planta functions of plant defensins and defensin-like peptides. Fungal Biol Rev 26:109–120CrossRefGoogle Scholar
  3. Fant F, Vranken W, Broekaert W, Borremans F (1998) Determination of the three-dimensional solution structure of Raphanus sativus antifungal protein 1 by 1H NMR. J Mol Biol 279:257–270CrossRefGoogle Scholar
  4. Howard RJ, Ferrari MA, Roach DH, Money NP (1991) Penetration of hard substrates by a fungus employing enormous turgor pressure. Proc Natl Acad Sci U S A 88:11281–11284CrossRefGoogle Scholar
  5. Jha S, Chattoo BB (2010) Expression of a plant defensin in rice confers resistance to fungal phytopathogens. Transgenic Res 19:373–384CrossRefGoogle Scholar
  6. Jha S, Tank HG, Prasad BD, Chattoo BB (2009) Expression of Dm-AMP1 in rice confers resistance to Magnaporthe oryzae and Rhizoctonia solani. Transgenic Res 18:59–96CrossRefGoogle Scholar
  7. Kanzaki H, Nirasawa S, Saitoh H, Ito M, Nishihara R, Nakamura I (2002) Overexpression of the wasabi defensin gene confers enhanced resistance to blast fungus (Magnaporthe grisea) in transgenic rice. Theor Appl Genet 105:809–814CrossRefGoogle Scholar
  8. Oguro Y, Yamazaki H, Takagi M, Takaku H (2014) Antifungal activity of plant defensin AFP1 in Brassica juncea involves the recognition of the methyl residue in glucosylceramide of target pathogen Candida albicans. Curr Genet 60:89–97CrossRefGoogle Scholar
  9. Poon IKH, Baxter AA, Lay FT, Mills GD, Adda CG, Payne JA, Phan TK, Ryan GF, White JA, Veneer PK, van der Weerden NL, Anderson MA, Kvansakul M, Hulett MD (2014) Phosphoinositide-mediated oligomerization of a defensin induces cell lysis. eLIFE 3:e01808CrossRefGoogle Scholar
  10. Sagehashi Y, Oguro Y, Tochihara T, Oikawa T, Tanaka H, Kawata M, Takagi M, Yatou O, Takaku H (2013) Purification and cDNA cloning of a defensin in Brassica juncea, its functional expression in Escherichia coli, and assessment of its antifungal activity. J Pestic Sci 38:33–38CrossRefGoogle Scholar
  11. Skamnioti T, Gurr SJ (2009) Against the grain: safeguarding rice from rice blast disease. Trends Biotechnol 27:141–150CrossRefGoogle Scholar
  12. Tam JP, Wamg S, Wong KH, Tan WL (2015) Antimicrobial peptides from plants. Pharmaceuticals 8:711–757CrossRefGoogle Scholar
  13. Terras FR, Schoofs HM, De Bolle MF, Van Leuven F, Rees SB, Vanderleyden J, Cammue BP, Broekaert WF (1992) Analysis of two novel classes of plant antifungal proteins from radish (Raphanus sativus L.) seeds. J Biol Chem 267:15301–15309PubMedGoogle Scholar
  14. Thevissen K, Terras FR, Broekaert WF (1999) Permeabilization of fungal membranes by plant defensins inhibits fungal growth. Appl Environ Microbiol 65:5451–5458PubMedPubMedCentralGoogle Scholar
  15. Thevissen K, Cammue BP, lemaire K, Winderickx J, Cickson RC, Lester RL, Ferket KK, Van Even F, Parret AH, Broekaert WF (2000) A gene encoding a sphingolipid biosynthesis enzyme determines the sensitivity of Saccharomyces cerevisiae to an antifungal plant defensin from dahlia (Dahlia merckii). Proc Natl Acad Sci U S A 97:9531–9536CrossRefGoogle Scholar
  16. Thevissen K, Warnecke DC, Francois IE, Leipelt M, Heinz E, Ott C, Zahringer U, Thomma BP, Ferket KK, Cammue BP (2004) Defensins from insects and plants interact fungal glucosylceramides. J Biol Chem 279:3900–3905CrossRefGoogle Scholar
  17. Vriens K, Cammue BP, Thevissen K (2014) Antifungal plant Defensins: mechanisms of action and production. Molecules 19:12280–12303CrossRefGoogle Scholar

Copyright information

© Società Italiana di Patologia Vegetale (S.I.Pa.V.) 2019

Authors and Affiliations

  • Yoshiyuki Sagehashi
    • 1
    Email author
  • Taketo Ashizawa
    • 2
  • Hiroaki Takaku
    • 3
  • Osamu Yatou
    • 4
  1. 1.Hokkaido Agricultural Research CenterNational Agriculture and Food Research OrganizationSapporoJapan
  2. 2.Central Region Agricultural Research CenterNational Agriculture and Food Research OrganizationTsukubaJapan
  3. 3.Department of Applied Life SciencesNiigata University of Pharmacy and Applied Life SciencesAkiha-kuJapan
  4. 4.Hokuriku Research Station, Central Region Agricultural Research CenterNational Agriculture and Food Research OrganizationJoetsuJapan

Personalised recommendations