ArticleBiochemistry2012
Structure and glycolipid binding properties of the nematicidal protein Cry5B.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 80 citations in OpenAlex.
- Interactions between insecticidal cry toxins and their receptors.Current genetics · 2025Review
- Essential Role of Non-Conserved α4-HisProtein and peptide letters · 2025Article
- Bacillus thuringiensis Cry14A family proteins as novel anthelmintics against gastrointestinal nematode parasites.PLoS neglected tropical diseases · 2024Article
- The nematode (Ascaris suum) intestine is a location of synergistic anthelmintic effects of Cry5B and levamisole.PLoS pathogens · 2024Article
- Biosynthesis of Cry5B-Loaded Sulfur Nanoparticles usingACS omega · 2024Article
- The role ofFrontiers in microbiology · 2024Review
- Channel Formation in Cry Toxins: An Alphafold-2 Perspective.International journal of molecular sciences · 2023Article
- The role of glycoconjugates as receptors for insecticidal proteins.FEMS microbiology reviews · 2023Review
- Aminopeptidase MNP-1 triggers intestine protease production by activating daf-16 nuclear location to degrade pore-forming toxins in Caenorhabditis elegans.PLoS pathogens · 2023Article
- Structural changes upon membrane insertion of the insecticidal pore-forming toxins produced byFrontiers in insect science · 2023Review
- The Crystal Structure ofToxins · 2022Article
- Insights from the Structure of an Active Form ofToxins · 2022Article
- A Caenorhabditis elegans nck-1 and filamentous actin-regulating protein pathway mediates a key cellular defense against bacterial pore-forming proteins.PLoS pathogens · 2022Article
- Function of CTLGA9 Amino Acid Residue Leucine-6 in Modulating Cry Toxicity.Frontiers in immunology · 2022Article
- Importance of Cry Proteins in Biotechnology: Initially a Bioinsecticide, Now a Vaccine Adjuvant.Life (Basel, Switzerland) · 2021Review
- Transcriptomic insights into the effects of CytCo, a novel nematotoxic protein, on the pine wood nematode Bursaphelenchus xylophilus.BMC genomics · 2021Article
- A new paraprobiotic-based treatment for control of Haemonchus contortus in sheep.International journal for parasitology. Drugs and drug resistance · 2020Article
- Rearrangement of N-Terminal α-Helices ofToxins · 2020Article
- Making 3D-Cry Toxin Mutants: Much More Than a Tool of Understanding Toxins Mechanism of Action.Toxins · 2020Review
- Crystal structure of Bacillus thuringiensis Cry7Ca1 toxin active against Locusta migratoria manilensis.Protein science : a publication of the Protein Society · 2019Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Crystal (Cry) proteins are globally used in agriculture as proteinaceous insecticides. They have also been recently recognized to have great potential as anthelmintic agents in targeting parasitic roundworms (e.g., hookworms). The most extensively characterized of the anthelmintic Cry proteins is Cry5B. We report here the 2.3 Å resolution structure of the proteolytically activated form of Cry5B. This structure, which is the first for a nematicidal Cry protein, shows the familiar three-domain arrangement seen in insecticidal Cry proteins. However, domain II is unusual in that it more closely resembles a banana lectin than it does other Cry proteins. This result is consistent with the fact that the receptor for Cry5B consists of a set of invertebrate-specific glycans (attached to lipids) and also suggests that domain II is important for receptor binding. We found that not only galactose but also N-acetylgalactosamine (GalNAc) is an efficient competitor for binding between Cry5B and glycolipids. GalNAc is one of the core arthroseries tetrasaccharides of the Cry5B receptor and galactose an antennary sugar that emanates from this core. These and prior data suggest that the minimal binding determinant for Cry5B consists of a core GalNAc and two antennary galactoses. Lastly, the protoxin form of Cry5B was found to bind nematode glycolipids with a specificity equal to that of activated Cry5B, but with lower affinity. This suggests that the initial binding of Cry5B protoxin to glycolipids can be stabilized at the nematode cell surface by proteolysis. These results lay the groundwork for the design of effective Cry5B-based anthelmintics.
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