ArticleThe Journal of biological chemistry2011
The structure of the elicitor Cerato-platanin (CP), the first member of the CP fungal protein family, reveals a double ψβ-barrel fold and carbohydrate binding.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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39 citing papers in PubMed, 114 citations in OpenAlex.
- Growth inhibition of arable weeds by cerato-platanin, a plant immune defense activator of fungal origin.Pest management science · 2025Article
- APlants (Basel, Switzerland) · 2025Article
- RmCP, a cerato-platanin protein fromFrontiers in microbiology · 2025Article
- Snowball: a novel gene family required for developmental patterning of fruiting bodies of mushroom-forming fungi (Agaricomycetes).mSystems · 2024Article
- Fused expression of Sm1-Chit42 proteins for synergistic mycoparasitic response of Trichoderma afroharzianum on Botrytis cinerea.Microbial cell factories · 2023Article
- Loosenin-Like Proteins fromApplied and environmental microbiology · 2023Article
- Structural characterization of a soil viral auxiliary metabolic gene product - a functional chitosanase.Nature communications · 2022Article
- Trichoderma harzianum cerato-platanin enhances hydrolysis of lignocellulosic materials.Microbial biotechnology · 2021Article
- The Evolutionary and Functional Paradox of Cerato-platanins in Fungi.Applied and environmental microbiology · 2020Article
- The two paralogous kiwellin proteins KWL1 and KWL1-b from maize are structurally related and have overlapping functions in plant defense.The Journal of biological chemistry · 2020Article
- Cerato-Platanins from Marine Fungi as Effective Protein Biosurfactants and Bioemulsifiers.International journal of molecular sciences · 2020Article
- Apoplastic Cell Death-Inducing Proteins of Filamentous Plant Pathogens: Roles in Plant-Pathogen Interactions.Frontiers in genetics · 2020Review
- KnotProt 2.0: a database of proteins with knots and other entangled structures.Nucleic acids research · 2019Article
- Plants fight fungi using kiwellin proteins.Nature · 2019Article
- Plants strike back: Kiwellin proteins as a modular toolbox for plant defense mechanisms.Communicative & integrative biology · 2019Article
- Topological knots and links in proteins.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- A single amino acid mutation affects elicitor and expansins-like activities of cerato-platanin, a non-catalytic fungal protein.PloS one · 2017Article
- Extracellular proteins of Trametes hirsuta st. 072 induced by copper ions and a lignocellulose substrate.BMC microbiology · 2016Article
- PAMP Activity of Cerato-Platanin during Plant Interaction: An -Omic Approach.International journal of molecular sciences · 2016Article
- The Cerato-Platanin protein Epl-1 from Trichoderma harzianum is involved in mycoparasitism, plant resistance induction and self cell wall protection.Scientific reports · 2015Article
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Authors and funding
10 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cerato-platanin (CP) is a secretion protein produced by the fungal pathogen Ceratocystis platani, the causal agent of the plane canker disease and the first member of the CP family. CP is considered a pathogen-associated molecular pattern because it induces various defense responses in the host, including production of phytoalexins and cell death. Although much is known about the properties of CP and related proteins as elicitors of plant defense mechanisms, its biochemical activity and host target(s) remain elusive. Here, we present the three-dimensional structure of CP. The protein, which exhibits a remarkable pH and thermal stability, has a double ψβ-barrel fold quite similar to those found in expansins, endoglucanases, and the plant defense protein barwin. Interestingly, although CP lacks lytic activity against a variety of carbohydrates, it binds oligosaccharides. We identified the CP region responsible for binding as a shallow surface located at one side of the β-barrel. Chemical shift perturbation of the protein amide protons, induced by oligo-N-acetylglucosamines of various size, showed that all the residues involved in oligosaccharide binding are conserved among the members of the CP family. Overall, the results suggest that CP might be involved in polysaccharide recognition and that the double ψβ-barrel fold is widespread in distantly related organisms, where it is often involved in host-microbe interactions.
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