Structural and functional analysis of the cerato-platanin-like protein Cpl1 suggests diverging functions in smut fungi
Abstract
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-Ψβ-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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BibTeX
@article{weiland2026structural,
title = {{Structural and functional analysis of the cerato-platanin-like protein Cpl1 suggests diverging functions in smut fungi}},
author = {Paul Weiland and Felix Dempwolff and Wieland Steinchen and Sven-Andreas Freibert and Hui Tian and Timo Glatter and Roman Martin and Bart P. H. J. Thomma and Gert Bange and Florian Altegoer},
journal = {Molecular Plant Pathology},
year = {2026},
month = oct,
doi = {10.1111/mpp.13349},
url = {https://hal.science/hal-05780519v1},
note = {CC BY-NC},
}
RIS
TY - JOUR
TI - Structural and functional analysis of the cerato-platanin-like protein Cpl1 suggests diverging functions in smut fungi
AU - Paul Weiland
AU - Felix Dempwolff
AU - Wieland Steinchen
AU - Sven-Andreas Freibert
AU - Hui Tian
AU - Timo Glatter
AU - Roman Martin
AU - Bart P. H. J. Thomma
AU - Gert Bange
AU - Florian Altegoer
PY - 2026
DA - 2026/10/06
JO - Molecular Plant Pathology
DO - 10.1111/mpp.13349
UR - https://hal.science/hal-05780519v1
AB - 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-Ψβ-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.
SN - 1464-6722
SN - 1364-3703
ER -