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Potent anti-HIV activity of scytovirin domain 1 peptide

  1. Author:
    Xiong, C. Y.
    O'Keefe, B. R.
    Byrd, R. A.
    McMahon, J. B.

  2. Author Address

    NCI, Mol Targets Dev Program, NIH, Frederick, MD 21702 USA. NCI, Struct Biophys Lab, NIH, Frederick, MD 21702 USA.;O'Keefe, BR, NCI, Mol Targets Dev Program, NIH, Bldg 562-Rm 201, Frederick, MD 21702 USA.;okeefe@ncifcrf.gov
    1. Year: 2006
    2. Date: Jul
  2. Journal: Peptides
    1. 27
    2. 7
    3. Pages: 1668-1675
  4. Type of Article: Article
  5. ISSN: 0196-9781
  1. Abstract:

    Scytovirin (SVN) is a novel anti-HIV protein isolated from aqueous extracts of the cultured cyanobacterium Scytonema varium. SVN contains two apparent domains, one comprising amino acids 1-48 and the second stretching from amino acids 49 to 95. These two domains display significant homology to each other and a similar pattern of disulfide bonds. Two DNA constructs encoding scytovirin 1-48 (Cys7Ser) (SD1) and 49-95 (Cys55Ser) (SD2) were constructed, and expressed in E. coli, with thioredoxin fused to their N-terminus. Purified recombinant products were tested for binding activities with the HIV surface envelope glycoproteins gp120 and gp41. Whole cell anti-HIV data showed that SDI had similar anti-HIV activity to the full-length SVN, whereas SD2 had significantly less anti-HIV activity. Further deletion mutants of the SD1 domain (SVN(3-45)Cys7Ser, SVN(6-45)Cys7Ser, SVN(11-45)Cys7Ser) showed that the N-terminal residues are necessary for full anti-HIV activity of SDI and that an eight amino acid deletion from the C-terminus (SVN(1-40)Cys7Ser) had a significant effect, decreasing the anti-HIV activity of SDI by approximately five-fold. Published by Elsevier Inc.

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External Sources

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  2. DOI: 10.1016/j.peptides.2006.03.018
  3. View record in Web of Science®
  4. WOS: 000238780300011

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