Change search
ReferencesLink to record
Permanent link

Direct link
Expression and beta-glucan binding properties of Scots pine (Pinus sylvestris L.) antimicrobial protein (Sp-AMP)
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
Show others and affiliations
2011 (English)In: Plant Molecular Biology, ISSN 0167-4412, E-ISSN 1573-5028, Vol. 77, no 1-2, 33-45 p.Article in journal (Refereed) Published
Abstract [en]

Scots pine (Pinus sylvestris) secretes a number of small, highly-related, disulfide-rich proteins (Sp-AMPs) in response to challenges with fungal pathogens such as Heterobasidion annosum, although their biological role has been unknown. Here, we examined the expression patterns of these genes, as well as the structure and function of the encoded proteins. Northern blots and quantitative real time PCR showed increased levels of expression that are sustained during the interactions of host trees with pathogens, but not non-pathogens, consistent with a function in conifer tree defenses. Furthermore, the genes were up-regulated after treatment with salicylic acid and an ethylene precursor, 1-aminocyclopropane-1-carboxylic-acid, but neither methyl jasmonate nor H(2)O(2) induced expression, indicating that Sp-AMP gene expression is independent of the jasmonic acid signaling pathways. The cDNA encoding one of the proteins was cloned and expressed in Pichia pastoris. The purified protein had antifungal activity against H. annosum, and caused morphological changes in its hyphae and spores. It was directly shown to bind soluble and insoluble beta-(1,3)-glucans, specifically and with high affinity. Furthermore, addition of exogenous glucan is linked to higher levels of Sp-AMP expression in the conifer. Homology modeling and sequence comparisons suggest that a conserved patch on the surface of the globular Sp-AMP is a carbohydrate-binding site that can accommodate approximately four sugar units. We conclude that these proteins belong to a new family of antimicrobial proteins (PR-19) that are likely to act by binding the glucans that are a major component of fungal cell walls.

Place, publisher, year, edition, pages
2011. Vol. 77, no 1-2, 33-45 p.
Keyword [en]
Antimicrobial protein, Heterobasidion annosum, beta-(1, 3)-glucan, Chitin, Inhibition, Binding, Homology modeling, Pathogen, Pinus sylvestris
National Category
Biological Sciences
URN: urn:nbn:se:uu:diva-158571DOI: 10.1007/s11103-011-9791-zISI: 000294200700003OAI: diva2:440546
Available from: 2011-09-13 Created: 2011-09-12 Last updated: 2015-04-23Bibliographically approved

Open Access in DiVA

fulltext(669 kB)50 downloads
File information
File name FULLTEXT01.pdfFile size 669 kBChecksum SHA-512
Type fulltextMimetype application/pdf

Other links

Publisher's full text

Search in DiVA

By author/editor
Mowbray, Sherry L.
By organisation
Department of Cell and Molecular BiologyStructure and Molecular Biology
In the same journal
Plant Molecular Biology
Biological Sciences

Search outside of DiVA

GoogleGoogle Scholar
Total: 50 downloads
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 205 hits
ReferencesLink to record
Permanent link

Direct link