Plant pathogenesis-related proteins of the cacao f... - BV FAPESP
Advanced search
Start date
Betweenand
Related content
(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Plant pathogenesis-related proteins of the cacao fungal pathogen Moniliophthora perniciosa differ in their lipid-binding specificities

Full text
Author(s):
Darwiche, Rabih [1] ; El Atab, Ola [1] ; Baroni, Renata M. [2, 3] ; Teixeira, Paulo J. P. L. [2] ; Mondego, Jorge M. C. [3] ; Pereira, Goncalo A. G. [2] ; Schneiter, Roger [1]
Total Authors: 7
Affiliation:
[1] Univ Fribourg, Div Biochem, Dept Biol, Chemin Musee 10, CH-1700 Fribourg - Switzerland
[2] Univ Estadual Campinas, Lab Genet & Expressao, BR-13083970 Campinas, SP - Brazil
[3] Inst Agron Campinas, BR-13083970 Campinas, SP - Brazil
Total Affiliations: 3
Document type: Journal article
Source: Journal of Biological Chemistry; v. 292, n. 50, p. 20558-20569, DEC 15 2017.
Web of Science Citations: 2
Abstract

Moniliophthora perniciosa is the causative agent of witches' broom disease, which devastates cacao cultures in South America. This pathogenic fungus infects meristematic tissues and derives nutrients from the plant apoplast during an unusually long-lasting biotrophic stage. To survive, the fungus produces proteins to suppress the plant immune response. Proteins of the PR-1 (pathogenesis-related 1)/CAP superfamily have been implicated in fungal virulence and immune suppression. The genome of M. perniciosa encodes 11 homologues of plant PR-1 proteins, designated MpPR-1 proteins, but their precise mode of action is poorly understood. In this study, we expressed MpPR-1 proteins in a yeast model lacking endogenous CAP proteins. We show that some members of the MpPR-1 family bind and promote secretion of sterols, whereas others bind and promote secretion of fatty acids. Lipid binding by purified MpPR-1 occurs with micromolar affinity and is saturable in vitro. Sterol binding by MpPR-1 requires the presence of a flexible loop region containing aromatic amino acids, the caveolin-binding motif. Remarkably, MpPR-1 family members that do not bind sterols can be converted to sterol binders by a single point mutation in the caveolin-binding motif. We discuss the possible implications of the lipid-binding activity of MpPR-1 family members with regard to the mode of action of these proteins during M. perniciosa infections. (AU)

FAPESP's process: 10/51884-8 - SMOLBnet 2.0: structural studies of key proteins for fungal diseases in cocoa: witch’s broom and moniliasis: developing strategies to control and understand the pathogenicity
Grantee:Andre Luis Berteli Ambrosio
Support Opportunities: Regular Research Grants
FAPESP's process: 12/07657-2 - PR-1 proteins and new receptor like kinases of cacao (Theobroma cacao): gene expression evaluation and search for ligands
Grantee:Jorge Maurício Costa Mondego
Support Opportunities: Regular Research Grants
FAPESP's process: 09/50119-9 - Integrated and comparative study of three fungal diseases of cacao: witches' broom, frosty pod rot and brown-rot, aiming at understanding the pathogenic mechanisms for the development of control strategies
Grantee:Gonçalo Amarante Guimarães Pereira
Support Opportunities: Research Projects - Thematic Grants