Biopolym. Cell. 2006; 22(2):126-131.
Structure and Function of Biopolymers
Characterization of defensin-like proteins from Scots pine seedlings
1Kovalyova V. A., 2Gout I. T., 1Gout R. T.
  1. National Forestry University of Ukraine
    103, General Chuprynky, Lviv, Ukraine, 79057
  2. University College London
    Gower Str., London WC1E 6BT, UK

Abstract

Two defensin-like proteins with molecular weight of 11.3 and 9.8 kDa were isolated from 7-day-old Scots pine seedlings (Pinus sylvestris L.) by the ion exchange chromatography on phosphocellulose. These proteins inhibited the growth of mycelium of the phytopathogenic fungus Fusarium oxysporum at concentration mkg/ml, and also caused the morphological changes of hyphae.
Keywords: Scots pine, defensin, Fusarium oxysporum

References

[1] Boman HG. Peptide antibiotics and their role in innate immunity. Annu Rev Immunol. 1995;13:61-92.
[2] Selitrennikoff CP. Antifungal proteins. Appl Environ Microbiol. 2001;67(7):2883-94.
[3] Terras FR, Eggermont K, Kovaleva V, Raikhel NV, Osborn RW, Kester A, Rees SB, Torrekens S, Van Leuven F, Vanderleyden J, et al. Small cysteine-rich antifungal proteins from radish: their role in host defense. Plant Cell. 1995;7(5):573-88.
[4] Cammue BP, De Bolle MF, Terras FR, Proost P, Van Damme J, Rees SB, Vanderleyden J, Broekaert WF. Isolation and characterization of a novel class of plant antimicrobial peptides form Mirabilis jalapa L. seeds. J Biol Chem. 1992;267(4):2228-33.
[5] Osborn RW, De Samblanx GW, Thevissen K, Goderis I, Torrekens S, Van Leuven F, Attenborough S, Rees SB, Broekaert WF. Isolation and characterisation of plant defensins from seeds of Asteraceae, Fabaceae, Hippocastanaceae and Saxifragaceae. FEBS Lett. 1995;368(2):257-62.
[6] Thomma BP, Cammue BP, Thevissen K. Plant defensins. Planta. 2002;216(2):193-202.
[7] Thevissen K, Ghazi A, De Samblanx GW, Brownlee C, Osborn RW, Broekaert WF. Fungal membrane responses induced by plant defensins and thionins. J Biol Chem. 1996;271(25):15018-25.
[8] Thevissen K, Ferket KK, François IE, Cammue BP. Interactions of antifungal plant defensins with fungal membrane components. Peptides. 2003;24(11):1705-12.
[9] Fossdal CG, Nagy NE, Sharma P, Lönneborg A. The putative gymnosperm plant defensin polypeptide (SPI1) accumulates after seed germination, is not readily released, and the SPI1 levels are reduced in Pythium dimorphum-infected spruce roots. Plant Mol Biol. 2003;52(2):291-302.
[10] Kovalyova VA, Cramer R, Gout IT, Gout RT. The analysis of tyrosine phosphorylation the process of seed germination of Scots pine. Ukr Biokhim Zh. 2005;77(2):119-20.
[11] Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227(5259):680-5.
[12] Shevchenko A, Wilm M, Vorm O, Mann M. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal Chem. 1996;68(5):850-8.
[13] Lam YW, Wang HX, Ng TB. A robust cysteine-deficient chitinase-like antifungal protein from inner shoots of the edible chive Allium tuberosum. Biochem Biophys Res Commun. 2000;279(1):74-80.
[14] Sundberg L, Porath J. Preparation of adsorbents for biospecific affinity chromatography. Attachment of group-containing ligands to insoluble polymers by means of bifuctional oxiranes. J Chromatogr. 1974;90(1):87-98.
[15] Fant F, Vranken W, Broekaert W, Borremans F. Determination of the three-dimensional solution structure of Raphanus sativus antifungal protein 1 by 1H NMR. J Mol Biol. 1998;279(1):257-70.
[16] Ozaki Y, Wada K, Hase T, Matsubara H, Nakanishi T, Yoshizumi H. Amino acid sequence of a purothionin homolog from barley flour. J Biochem. 1980;87(2):549-55.
[17] Segura A, Moreno M, Molina A, García-Olmedo F. Novel defensin subfamily from spinach (Spinacia oleracea). FEBS Lett. 1998;435(2-3):159-62.