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Abstract

Scots pine (Pinus sylvestris) produces several small, highly homologous, disulfide-rich proteins (Sp-AMPs) in response to fungal pathogenic attacks. We report here the expression, structure and function of these proteins. One of the Sp-AMPs was cloned into and over-expressed in Pichia pastoris. The purified protein shows antifungal activity against Heterobasidion annosum, causing morphological changes in spores and hyphae. Binding studies revealed that it binds to soluble and insoluble beta-(1,3)-glucans, major components of the fungal cell wall, with high affinity. Homology modeling studies suggest a Greek-key-beta-barrel fold having a conserved patch on the surface that can accommodate at least 4 sugar units. We conclude that these proteins represent a new class of antimicrobial proteins that can be classified as pathogenesis related (PR) protein family 18.

Keywords

antimicrobial proteins; beta-(1,3)-glucan; binding; Heterobasidion annosum; homology modelling; inhibition; pathogen; Pinus sylvestris

Published in

Title: Science and Technology Against Microbial Pathogens Research, Development and Evaluation Proceedings of the International Conference on Antimicrobial Research (ICAR2010), Valladolid, Spain, 3 – 5 November 2010
Publisher: World scientific

Conference

International Conference on Antimicrobial Research, NOV 03-05, 2010, Valladolid, SPAIN

SLU Authors

  • Sooriyaarachchi, Sanjeewani

    • Department of Molecular Biology, Swedish University of Agricultural Sciences

  • Ubhayasekera, Wimal

    • Department of Molecular Biology, Swedish University of Agricultural Sciences

  • Mowbray, Sherry

    • Department of Molecular Biology, Swedish University of Agricultural Sciences
    • Uppsala University

UKÄ Subject classification

Molecular Biology
Biochemistry

Publication identifier

  • ISBN: 978-981-4354-85-1

Permanent link to this page (URI)

https://res.slu.se/id/publ/118113