Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/37950
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | Fungal cell wall phosphomannans facilitate the toxic activity of a plant PR-5 protein |
Autor: | Ibeas, José I. CSIC ORCID; Lee, Hyeseung; Damsz, Barbara; Prasad, Doddananjappa T.; Pardo, José M. CSIC ORCID ; Hasegawa, Paul M.; Bressan, Ray A.; Narasimhan, Meena L. | Palabras clave: | Cell walls Fungal Mannan Pathogenesis-related protein Saccharomyces cerevisiae Thamatin-like |
Fecha de publicación: | ago-2000 | Editor: | Wiley-Blackwell | Citación: | Plant Journal 23 (3): 375-383 (2000) | Resumen: | Osmotin is a plant PR-5 protein. It has a broad spectrum of antifungal activity, yet also exhibits specificity for certain fungal targets. The structural bases for this specificity remain unknown. We show here that full sensitivity of Saccharomyces cerevisiae cells to the PR-5 protein osmotin is dependent on the function of MNN2, MNN4 and MNN6. MNN2 is an α-1,2-mannosyltransferase catalyzing the addition of the first mannose to the branches on the poly l,6-mannose backbone of the outer chain of cell wall N-linked mannans. MNN4 and MNN6 are required for the transfer of mannosylphosphate to cell wall mannans. Null mnn2, mnn4 or mnn6 mutants lack phosphomannans and are defective in binding osmotin to the fungal cell wall. Both antimannoprotein antibody and the cationic dye alcian blue protect cells against osmotin cytotoxicity. MNN1 is an α-1,3-mannosyltransferase that adds the terminal mannose to the outer chain branches of N-linked mannan, masking mannosylphosphate. Null mnn1 cells exhibit enhanced osmotin binding and sensitivity. Several cell wall mannoproteins can bind to immobilized osmotin, suggesting that their polysaccharide constituent determines osmotin binding. Our results demonstrating a causal relationship between cell surface phosphomannan and the susceptibility of a yeast strain to osmotin suggest that cell surface polysaccharides of invading pathogens control target specificity of plant PR-5 proteins. | Descripción: | 9 pages, 6 figures, 1 table, 35 references. | Versión del editor: | http://dx.doi.org/10.1046/j.1365-313x.2000.00792.x | URI: | http://hdl.handle.net/10261/37950 | DOI: | 10.1046/j.1365-313x.2000.00792.x | ISSN: | 0960-7412 |
Aparece en las colecciones: | (IRNAS) Artículos |
Mostrar el registro completo
CORE Recommender
WEB OF SCIENCETM
Citations
80
checked on 22-feb-2024
Page view(s)
320
checked on 18-abr-2024
Google ScholarTM
Check
Altmetric
Altmetric
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.