Cyanovirin-N

Cyanovirin-N (CV-N) is a protein produced by the cyanobacterium that displays virucidal activity against several viruses, including human immunodeficiency virus (HIV).^[1] The virucidal activity of CV-N is mediated through specific high-affinity interactions with the viral surface envelope glycoproteins gp120 and gp41, as well as to high-mannose oligosaccharides found on the HIV envelope.^[2] In addition, CV-N is active against rhinoviruses, human parainfluenza virus, respiratory syncytial virus, and enteric viruses. The virucidal activity of CV-N against influenza virus is directed towards viral haemagglutinin.^[3] CV-N has a complex fold composed of a duplication of a tandem repeat of two homologous motifs comprising three-stranded beta-sheet and beta-hairpins.^[4]

Professor Julian Ma of St George's Hospital, South London, has a project in Kent, England to use genetically modified tobacco plants to produce the Cyanovirin and from this produce a cream which could be used to prevent HIV infection^{[citation needed]}

Cyanovirin is a protein with a highly complicated structure, it binds to sugars attached to HIV, it envelopes the protein and prevents it from binding to the mucosal cell surfaces in the Vagina and Rectum, this compound is also active against herpes viruses.^{[citation needed]}

"Development of cyanovirin has been exceedingly slow-paced. The chief of the NCI cyanovirin program, Michael Boyd, described it as "languishing." Apparently the NCI's production facilities, based on genetically manipulated cell cultures, have been diverted to other projects that the agency considers of higher priority. This is unfortunate: cyanovirin is of particular interest because of its relative safety. It is 10,000 times more toxic to HIV than it is to cells."^{[citation needed]}

This protein may use the morpheein model of allosteric regulation.^[5]

References[]

^ Zappe H, Snell ME, Bossard MJ (2008). "PEGylation of cyanovirin-N, an entry inhibitor of HIV". Adv. Drug Deliv. Rev. 60 (1): 79–87. doi:10.1016/j.addr.2007.05.016. PMID 17884238.
^ Botos I, Wlodawer A (February 2003). "Cyanovirin-N: a sugar-binding antiviral protein with a new twist". Cell. Mol. Life Sci. 60 (2): 277–87. doi:10.1007/s000180300023. PMID 12678493. S2CID 10579615.
^ O'Keefe BR, Smee DF, Turpin JA, Saucedo CJ, Gustafson KR, Mori T, Blakeslee D, Buckheit R, Boyd MR (August 2003). "Potent anti-influenza activity of cyanovirin-N and interactions with viral hemagglutinin". Antimicrob. Agents Chemother. 47 (8): 2518–25. doi:10.1128/aac.47.8.2518-2525.2003. PMC 166092. PMID 12878514.
^ Botos I, O'Keefe BR, Shenoy SR, Cartner LK, Ratner DM, Seeberger PH, Boyd MR, Wlodawer A (September 2002). "Structures of the complexes of a potent anti-HIV protein cyanovirin-N and high mannose oligosaccharides". J. Biol. Chem. 277 (37): 34336–42. doi:10.1074/jbc.M205909200. PMID 12110688.
^ T. Selwood & E. K. Jaffe (2011). "Dynamic dissociating homo-oligomers and the control of protein function". Arch. Biochem. Biophys. 519 (2): 131–43. doi:10.1016/j.abb.2011.11.020. PMC 3298769. PMID 22182754.

External links[]

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[pmid17884238-1] Zappe H, Snell ME, Bossard MJ (2008). "PEGylation of cyanovirin-N, an entry inhibitor of HIV". Adv. Drug Deliv. Rev. 60 (1): 79–87. doi:10.1016/j.addr.2007.05.016. PMID 17884238.

[pmid12678493-2] Botos I, Wlodawer A (February 2003). "Cyanovirin-N: a sugar-binding antiviral protein with a new twist". Cell. Mol. Life Sci. 60 (2): 277–87. doi:10.1007/s000180300023. PMID 12678493. S2CID 10579615.

[pmid12878514-3] O'Keefe BR, Smee DF, Turpin JA, Saucedo CJ, Gustafson KR, Mori T, Blakeslee D, Buckheit R, Boyd MR (August 2003). "Potent anti-influenza activity of cyanovirin-N and interactions with viral hemagglutinin". Antimicrob. Agents Chemother. 47 (8): 2518–25. doi:10.1128/aac.47.8.2518-2525.2003. PMC 166092. PMID 12878514.

[pmid12110688-4] Botos I, O'Keefe BR, Shenoy SR, Cartner LK, Ratner DM, Seeberger PH, Boyd MR, Wlodawer A (September 2002). "Structures of the complexes of a potent anti-HIV protein cyanovirin-N and high mannose oligosaccharides". J. Biol. Chem. 277 (37): 34336–42. doi:10.1074/jbc.M205909200. PMID 12110688.

[pmid22182754-5] T. Selwood & E. K. Jaffe (2011). "Dynamic dissociating homo-oligomers and the control of protein function". Arch. Biochem. Biophys. 519 (2): 131–43. doi:10.1016/j.abb.2011.11.020. PMC 3298769. PMID 22182754.

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