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Structural and functional analysis of the cerato-platanin-like protein Cpl1 suggests diverging functions in smut fungi.
Weiland, Paul; Dempwolff, Felix; Steinchen, Wieland; Freibert, Sven-Andreas; Tian, Hui; Glatter, Timo; Martin, Roman; Thomma, Bart P H J; Bange, Gert; Altegoer, Florian.
Afiliación
  • Weiland P; Center for Synthetic Microbiology (SYNMIKRO), Faculty of Chemistry, Philipps-University Marburg, Marburg, Germany.
  • Dempwolff F; Center for Synthetic Microbiology (SYNMIKRO), Faculty of Chemistry, Philipps-University Marburg, Marburg, Germany.
  • Steinchen W; Center for Synthetic Microbiology (SYNMIKRO), Faculty of Chemistry, Philipps-University Marburg, Marburg, Germany.
  • Freibert SA; Center for Synthetic Microbiology (SYNMIKRO), Institute of Cytobiology, Philipps-University Marburg, Marburg, Germany.
  • Tian H; Protein Biochemistry and Spectroscopy Core Facility, Institute of Cytobiology, Philipps-University Marburg, Marburg, Germany.
  • Glatter T; Institute for Plant Sciences, University of Cologne, Cologne, Germany.
  • Martin R; Max-Planck Institute for Terrestrial Microbiology, Marburg, Germany.
  • Thomma BPHJ; Faculty of Mathematics and Computer Science, Philipps-University Marburg, Marburg, Germany.
  • Bange G; Institute for Plant Sciences, University of Cologne, Cologne, Germany.
  • Altegoer F; Cluster of Excellence on Plant Sciences (CEPLAS), Cologne, Germany.
Mol Plant Pathol ; 24(7): 768-787, 2023 07.
Article en En | MEDLINE | ID: mdl-37171083
Plant-pathogenic fungi are causative agents of the majority of plant diseases and can lead to severe crop loss in infected populations. Fungal colonization is achieved by combining different strategies, such as avoiding and counteracting the plant immune system and manipulating the host metabolome. Of major importance are virulence factors secreted by fungi, which fulfil diverse functions to support the infection process. Most of these proteins are highly specialized, with structural and biochemical information often absent. Here, we present the atomic structures of the cerato-platanin-like protein Cpl1 from Ustilago maydis and its homologue Uvi2 from Ustilago hordei. Both proteins adopt a double-Ψß-barrel architecture reminiscent of cerato-platanin proteins, a class so far not described in smut fungi. Our structure-function analysis shows that Cpl1 binds to soluble chitin fragments via two extended grooves at the dimer interface of the two monomer molecules. This carbohydrate-binding mode has not been observed previously and expands the repertoire of chitin-binding proteins. Cpl1 localizes to the cell wall of U. maydis and might synergize with cell wall-degrading and decorating proteins during maize infection. The architecture of Cpl1 harbouring four surface-exposed loop regions supports the idea that it might play a role in the spatial coordination of these proteins. While deletion of cpl1 has only mild effects on the virulence of U. maydis, a recent study showed that deletion of uvi2 strongly impairs U. hordei virulence. Our structural comparison between Cpl1 and Uvi2 reveals sequence variations in the loop regions that might explain a diverging function.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ustilaginales / Ustilago / Plumbaginaceae Idioma: En Revista: Mol Plant Pathol Año: 2023 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido
Texto completo
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Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ustilaginales / Ustilago / Plumbaginaceae Idioma: En Revista: Mol Plant Pathol Año: 2023 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido