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

  • Darwiche R From the Division of Biochemistry, Department of Biology, University of Fribourg, 1700 Fribourg, Switzerland.
  • El Atab O From the Division of Biochemistry, Department of Biology, University of Fribourg, 1700 Fribourg, Switzerland.
  • Baroni RM the Instituto Agronômico de Campinas, Campinas, SP 13083-970, Brazil, and.
  • Teixeira PJPL the Laboratório de Genética e Expressão, UNICAMP, Campinas, São Paulo 13083-970, Brazil.
  • Mondego JMC the Instituto Agronômico de Campinas, Campinas, SP 13083-970, Brazil, and.
  • Pereira GAG the Laboratório de Genética e Expressão, UNICAMP, Campinas, São Paulo 13083-970, Brazil goncalo@unicamp.br.
  • Schneiter R From the Division of Biochemistry, Department of Biology, University of Fribourg, 1700 Fribourg, Switzerland, roger.schneiter@unifr.ch.
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  • 2017-10-19
Published in:
  • The Journal of biological chemistry. - 2017
fatty acid
fatty acid binding protein
infection
lipid-protein interaction
sterol
Agaricales
Amino Acid Motifs
Amino Acid Sequence
Amino Acid Substitution
Binding, Competitive
Cacao
Cholesterol
Fatty Acids, Nonesterified
Fungal Proteins
Gene Deletion
Kinetics
Ligands
Mutagenesis, Site-Directed
Palmitic Acid
Point Mutation
Protein Conformation
Protein Isoforms
Sterols
English 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.
Language
  • English
Open access status
bronze
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https://sonar.ch/global/documents/138959
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