Cyanovirin-N: a sugar-binding antiviral protein with a new twist

@article{Botos2003CyanovirinNAS,
  title={Cyanovirin-N: a sugar-binding antiviral protein with a new twist},
  author={Istvan Botos and Alexander Wlodawer},
  journal={Cellular and Molecular Life Sciences CMLS},
  year={2003},
  volume={60},
  pages={277-287}
}
Abstract. Cyanovirin-N (CV-N), an 11-kDa protein from the cyanobacterium Nostoc ellipsosporum, is a highly potent virucidal agent that has generated interest as a lead natural product for the prevention and chemotherapy of human immunodeficiency virus infection. The antiviral activity of CV-N is mediated through specific, high-affinity interactions with the viral surface envelope glycoproteins. A number of structures of wild-type, mutant and sequence-shuffled CV-N have been solved by nuclear… 
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TLDR
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TLDR
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TLDR
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TLDR
The structure and activity of the most promising antiviral cyanobacterial products are presented and provide a good basis for further studies on the therapeutic potential of these microorganisms.
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The solution structure of cyanovirin-N, a potent 11,000 M r HIV-inactivating protein that binds with high affinity and specificity to the HIV surface envelope protein gp120, has been solved by
Domain-swapped structure of a mutant of cyanovirin-N.
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TLDR
CV-N binds with extremely high affinity to highly conserved binding site(s) on the viral envelope glycoprotein gp120, preventing virus-to-cell fusion, viral entry and infection of cells, and is undergoing preclinical development for topical anti-HIV prophylactic applications to prevent sexual transmission of HIV.
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TLDR
An obligate domain-swapped dimer of cyanovirin-N is constructed that represents a new tetravalent carbohydrate binding protein that is stable over a large range of pH values and can be rapidly obtained in >98% purity in a single chromatographic step.
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TLDR
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TLDR
The crystal structure of cyanovirin-N (CV-N), a protein with potent antiviral activity, was solved at 1.5 A resolution by molecular replacement using as the search model the solution structure previously determined by NMR, with the exception of the unexpected phenomenon of domain swapping.
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TLDR
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TLDR
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TLDR
This recombinant production and purification of a novel anti-human immunodeficiency virus (HIV) protein, cyanovirin-N (CV-N), in Escherichia coli provides a basis for large-scale production of clinical grade CV-N for further research and development as an anti-HIV microbicide.
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