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Overexpression and purification of scytovirin, a potent, novel anti-HIV protein from the cultured cyanobacterium Scytonema varium

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

  2. Author Address

    NCI, Mol Targets Dev Program, NIH, Frederick, MD 21701 USA. NCI, Prot Struct Sect, Macromol Crystallog Lab, Frederick, MD 21701 USA.;O'Keefe, BR, NCI, Mol Targets Dev Program, NIH, Frederick, MD 21701 USA.;okeefe@ncifcrf.gov
    1. Year: 2006
    2. Date: Apr
  2. Journal: Protein Expression and Purification
    1. 46
    2. 2
    3. Pages: 233-239
  4. Type of Article: Article
  5. ISSN: 1046-5928
  1. Abstract:

    Scytovirin (SVN) is a novel anti-human immunodeficiency virus (HIV) protein isolated from aqueous extracts of the cultured cyanobacterium Scytonema varium. The protein consists of a single 95-amino acid chain with significant internal sequence duplication and 10 cysteines forming five intrachain disulfide bonds. A synthetic gene that encodes scytovirin was constructed, and expressed in Escherichia coli, with thioredoxin (TRX) fused to its N-terminus (TRX-SVN). Most of the expressed protein was in soluble form, which was purified by a polyhistidine tag affinity purification step. SVN was then cleaved from TRX with enterokinase and separated from the TRX partner by C18 reversed-phase HPLC. This production method has proven superior to earlier synthetic attempts and recombinant procedures using a standard expression system. The current system resulted in yields of 5-10 mg/L of purified SVN for structural studies and for preclinical development of SVN as a topical microbicide for HIV prophylaxis. Published by Elsevier Inc.

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External Sources

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  2. DOI: 10.1016/j.pep.2005.09.019
  3. View record in Web of Science®
  4. WOS: 000236828100008

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