Cyanovirin-N Explained

Cyanovirin-N (CV-N) is a protein produced by the cyanobacterium Nostoc ellipsosporum that displays virucidal activity against several viruses, including human immunodeficiency virus (HIV).[1] A cyanobacterial protein called cyanovirin-N (CV-N) has strong anti-human immunodeficiency virus (HIV) neutralizing properties.[2] 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.[3] 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.[4]

The blue-green alga Nostoc ellipsosporum naturally contains the protein cyanovirin-N. The National Cancer Institute (NCI) in the United States carried out the initial isolation and characterisation of this protein in 1999.[5] The use of cyanovirin-N as an antiviral drug, particularly against HIV, has since been the subject of investigation. Its ability to bind to the HIV-encapsulating glycoprotein gp120 has been demonstrated in several studies, which has led to the development of Cyanovirin-N-based therapies and preventatives.[5]

Structure

Cyanovirin-N is a lengthy, mostly beta-sheet protein that displays internal two-fold pseudosymmetry. The fundamental atomic root-mean-square of the two sequence repeats (1-50 and 51-101) differs by 1.3 A while sharing 32% of the same sequence. The total fold depends on a number of interactions between the two repetitions, therefore they don't actually belong in separate domains.[6] 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.[7]

References

  1. Zappe H, Snell ME, Bossard MJ . PEGylation of cyanovirin-N, an entry inhibitor of HIV . Adv. Drug Deliv. Rev. . 60 . 1 . 79–87 . 2008 . 17884238 . 10.1016/j.addr.2007.05.016 .
  2. Dey, Barna, Danica L. Lerner, Paolo Lusso, Michael R. Boyd, John H. Elder, and Edward A. Berger. “Multiple Antiviral Activities of Cyanovirin-N: Blocking of Human Immunodeficiency Virus Type 1 gp120 Interaction with CD4 and Coreceptor and Inhibition of Diverse Enveloped Viruses.” Journal of Virology 74, no. 10 (2000): 4562–69. https://doi.org/10.1128/jvi.74.10.4562-4569.2000.)
  3. Botos I, Wlodawer A . Cyanovirin-N: a sugar-binding antiviral protein with a new twist . Cell. Mol. Life Sci. . 60 . 2 . 277–87 . February 2003 . 12678493 . 10.1007/s000180300023. 10579615 . 11138712 .
  4. O'Keefe BR, Smee DF, Turpin JA, Saucedo CJ, Gustafson KR, Mori T, Blakeslee D, Buckheit R, Boyd MR . Potent anti-influenza activity of cyanovirin-N and interactions with viral hemagglutinin . Antimicrob. Agents Chemother. . 47 . 8 . 2518–25 . August 2003 . 12878514 . 166092 . 10.1128/aac.47.8.2518-2525.2003.
  5. Boyd. MR. Gustafson. KR. McMahon. JB. Shoemaker. RH. O'Keefe. BR. Mori. T. Gulakowski. RJ. Wu. L. Rivera. MI. Laurencot. CM. Currens. MJ. Cardellina. JH 2nd. Buckheit. RW Jr. Nara. PL. Pannell. LK. Sowder. RC 2nd. Henderson. LE. Discovery of cyanovirin-N, a novel human immunodeficiency virus-inactivating protein that binds viral surface envelope glycoprotein gp120: potential applications to microbicide development. Antimicrobial Agents and Chemotherapy. June 1997. 41. 6. 1521–1530. 10.1128/AAC.41.7.1521. 9210678 . 5. 163952.
  6. Bewley. C.. Gustafson. K.. Boyd. M.. D.G.. Covell. A.. Bax. G.M.. Clore. A.M.. Gronenborn. Solution structure of cyanovirin-N, a potent HIV-inactivating protein. Nature Structural and Molecular Biology. 5. 571–578. 1998. 7 . 10.1038/828. 9665171 . 11367037 .
  7. Botos I, O'Keefe BR, Shenoy SR, Cartner LK, Ratner DM, Seeberger PH, Boyd MR, Wlodawer A . Structures of the complexes of a potent anti-HIV protein cyanovirin-N and high mannose oligosaccharides . J. Biol. Chem. . 277 . 37 . 34336–42 . September 2002 . 12110688 . 10.1074/jbc.M205909200 . free .

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