A new class of Scots pine antimicrobial proteins, which act by binding beta-glucan

Sanjeewani Sooriyaarachchi; Adrian Suarez Covarrubias; Wimal Ubhayasekera; Frederick O. Asiegbu; Sherry Mowbray

A new class of Scots pine antimicrobial proteins, which act by binding beta-glucan

Sanjeewani Sooriyaarachchi
, Adrian Suarez Covarrubias
, Wimal Ubhayasekera
, Frederick O. Asiegbu
, Sherry Mowbray

Publication: Chapter in Book/Report/Conference proceeding › Conference paper in proceedings › peer-review

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.

Original language	English
Title of host publication	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
Pages	3-6
Number of pages	4
ISBN (Print)	978-981-4354-85-1
Publication status	Published - 2011

Keywords

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

Cite this

Sooriyaarachchi, S., Covarrubias, A. S., Ubhayasekera, W., Asiegbu, F. O., & Mowbray, S. (2011). A new class of Scots pine antimicrobial proteins, which act by binding beta-glucan. In 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 (pp. 3-6). World Scientific.

Sooriyaarachchi, Sanjeewani ; Covarrubias, Adrian Suarez ; Ubhayasekera, Wimal et al. / A new class of Scots pine antimicrobial proteins, which act by binding beta-glucan. 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. World Scientific, 2011. pp. 3-6

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title = "A new class of Scots pine antimicrobial proteins, which act by binding beta-glucan",

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

author = "Sanjeewani Sooriyaarachchi and Covarrubias, \{Adrian Suarez\} and Wimal Ubhayasekera and Asiegbu, \{Frederick O.\} and Sherry Mowbray",

year = "2011",

language = "English",

isbn = "978-981-4354-85-1",

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Sooriyaarachchi, S, Covarrubias, AS, Ubhayasekera, W, Asiegbu, FO & Mowbray, S 2011, A new class of Scots pine antimicrobial proteins, which act by binding beta-glucan. in 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. World Scientific, pp. 3-6.

A new class of Scots pine antimicrobial proteins, which act by binding beta-glucan. / Sooriyaarachchi, Sanjeewani; Covarrubias, Adrian Suarez; Ubhayasekera, Wimal et al.
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. World Scientific, 2011. p. 3-6.

Publication: Chapter in Book/Report/Conference proceeding › Conference paper in proceedings › peer-review

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T1 - A new class of Scots pine antimicrobial proteins, which act by binding beta-glucan

AU - Sooriyaarachchi, Sanjeewani

AU - Covarrubias, Adrian Suarez

AU - Ubhayasekera, Wimal

AU - Asiegbu, Frederick O.

AU - Mowbray, Sherry

PY - 2011

Y1 - 2011

N2 - 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.

AB - 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.

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KW - Pinus sylvestris

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KW - beta-(1,3)-glucan

KW - binding

KW - homology modelling

KW - inhibition

KW - pathogen

KW - Heterobasidion annosum

KW - Pinus sylvestris

KW - antimicrobial proteins

KW - beta-(1,3)-glucan

KW - binding

KW - homology modelling

KW - inhibition

KW - pathogen

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SN - 978-981-4354-85-1

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BT - 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

PB - World Scientific

ER -

Sooriyaarachchi S, Covarrubias AS, Ubhayasekera W, Asiegbu FO, Mowbray S. A new class of Scots pine antimicrobial proteins, which act by binding beta-glucan. In 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. World Scientific. 2011. p. 3-6

A new class of Scots pine antimicrobial proteins, which act by binding beta-glucan

Abstract

Keywords

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