ArticleStructure (London, England : 1993)2011
Structure-function analysis of a CVNH-LysM lectin expressed during plant infection by the rice blast fungus Magnaporthe oryzae.
Article in Structure (London, England : 1993), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 55 citations in OpenAlex.
- Structural and Functional Analysis of the Lectin-like Protein Llp1 Secreted byJournal of fungi (Basel, Switzerland) · 2025Article
- Review
- Genome Analysis of the Broad Host Range NecrotrophFrontiers in plant science · 2022Article
- The Pleiades are a cluster of fungal effectors that inhibit host defenses.PLoS pathogens · 2021Article
- A secreted LysM effector protects fungal hyphae through chitin-dependent homodimer polymerization.PLoS pathogens · 2020Article
- Article
- Integrating NMR, SAXS, and Atomistic Simulations: Structure and Dynamics of a Two-Domain Protein.Biophysical journal · 2018Article
- Article
- Transcriptome analysis reveals a complex interplay between resistance and effector genes during the compatible lentil-Colletotrichum lentis interaction.Scientific reports · 2017Article
- Article
- Structural Insight into Fungal Cell Wall Recognition by a CVNH Protein with a Single LysM Domain.Structure (London, England : 1993) · 2015Article
- Molecular diversity of LysM carbohydrate-binding motifs in fungi.Current genetics · 2015Review
- An intermolecular binding mechanism involving multiple LysM domains mediates carbohydrate recognition by an endopeptidase.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Fungi on the skin: dermatophytes and Malassezia.Cold Spring Harbor perspectives in medicine · 2014Review
- Molecular basis for bacterial peptidoglycan recognition by LysM domains.Nature communications · 2014Article
- Cloning, expression, purification, crystallization and preliminary crystallographic analysis of the putative NlpC/P60 endopeptidase, TTHA0266, from Thermus thermophilus HB8.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- An introduction to biological NMR spectroscopy.Molecular & cellular proteomics : MCP · 2013Review
- Article
- Sweet entanglements--protein:glycan interactions in two HIV-inactivating lectin families.Biopolymers · 2013Review
- Article
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
Abstract
The rice blast fungus Magnaporthe oryzae's genome encodes a hypothetical protein (MGG_03307) containing a type III CVNH lectin, in which a LysM domain is inserted between individual repeats of a single CVNH domain. At present, no structural or ligand binding data are available for any type III CVNH and functional studies in natural source organisms are scarce. Here, we report NMR solution structure and functional data on MGG_03307. The structure of the CVNH/LysM module revealed that intact and functionally competent CVNH and LysM domains are present. Using NMR titrations, carbohydrate specificities for both domains were determined, and it was found that each domain behaves as an isolated unit without any interdomain communication. Furthermore, live-cell imaging revealed a predominant localization of MGG_03307 within the appressorium, the specialized fungal cell for gaining entry into rice tissue. Our results suggest that MGG_03307 plays a role in the early stages of plant infection.
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