ArticleJournal of molecular biology2007
The novel fold of scytovirin reveals a new twist for antiviral entry inhibitors.
Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
27 citing papers in PubMed, 55 citations in OpenAlex.
- Article
- Production of Plant Proteins and Peptides with Pharmacological Potential.Advances in biochemical engineering/biotechnology · 2024Review
- The Antiviral Potential of Algal Lectins.Marine drugs · 2023Review
- Lectins and lectibodies: potential promising antiviral agents.Cellular & molecular biology letters · 2022Review
- Physicochemical characterization of the recombinant lectin scytovirin and microbicidal activity of the SD1 domain produced in rice against HIV-1.Plant cell reports · 2022Article
- Polyphasic evaluation and cytotoxic investigation of isolated cyanobacteria with an emphasis on potent activities of aFrontiers in microbiology · 2022Article
- Structural Insight into the Binding of Cyanovirin-N with the Spike Glycoprotein, MMolecules (Basel, Switzerland) · 2021Article
- Antiviral Cyanometabolites-A Review.Biomolecules · 2021Review
- An off-the-Shelf Approach for the Production of Fc Fusion Proteins by ProteinInternational journal of molecular sciences · 2020Article
- Overview of the Structure⁻Function Relationships of Mannose-Specific Lectins from Plants, Algae and Fungi.International journal of molecular sciences · 2019Review
- Plant-derived antivirals against hepatitis c virus infection.Virology journal · 2018Review
- In silico analysis of the cyanobacterial lectin scytovirin: new insights into binding properties.Molecular biology reports · 2017Article
- Antiviral lectins: Selective inhibitors of viral entry.Antiviral research · 2017Review
- Novel Antifungal Activity for the Lectin Scytovirin: Inhibition ofFrontiers in microbiology · 2017Article
- Bacterial production of site specificJournal of biomolecular NMR · 2017Article
- Uncovering Potential Applications of Cyanobacteria and Algal Metabolites in Biology, Agriculture and Medicine: Current Status and Future Prospects.Frontiers in microbiology · 2017Review
- HIV-1 gp120 as a therapeutic target: navigating a moving labyrinth.Expert opinion on therapeutic targets · 2015Review
- Lectins with anti-HIV activity: a review.Molecules (Basel, Switzerland) · 2015Review
- The cyanobacterial lectin scytovirin displays potent in vitro and in vivo activity against Zaire Ebola virus.Antiviral research · 2014Article
- Using glycan microarrays to understand immunity.Current opinion in chemical biology · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
The solution structure of the potent 95 residue anti-HIV protein scytovirin has been determined and two carbohydrate-binding sites have been identified. This unique protein, containing five structurally important disulfide bonds, demonstrates a novel fold with no elements of extended regular secondary structure. Scytovirin contains two 39 residue sequence repeats, differing in only three amino acid residues, and each repeat has primary sequence similarity to chitin binding proteins. Both sequence repeats form similarly structured domains, with the exception of one region. The result is two carbohydrate-binding sites with substantially different affinities. The unusual fold clusters aromatic residues in both sites, suggesting a binding mechanism similar to other known hevein-like carbohydrate-binding proteins but differing in carbohydrate specificity. Scytovirin, originally isolated from the cyanobacterium Scytonema varium, holds potential as an HIV entry inhibitor for both therapeutic and prophylactic anti-HIV applications. The high-resolution structural studies reported are an important initial step in unlocking the therapeutic potential of scytovirin.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.