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Functional homologs of cyanovirin-N amenable to mass production in prokaryotic and eukaryotic hosts

  1. Author:
    Mori, T.
    Barrientos, L. G.
    Han, Z. Z.
    Gronenborn, A. M.
    Turpin, J. A.
    Boyd, M. R.

  2. Author Address

    NCI, Canc Res Ctr, Mol Targets Drug Discovery Program, Frederick, MD 21702 USA NCI, Canc Res Ctr, Mol Targets Drug Discovery Program, Frederick, MD 21702 USA NIDDKD, Phys Chem Lab, NIH, Bethesda, MD 20892 USA So Res Inst, Infect Dis Res Dept, Frederick, MD 21701 USA Mori T NCI, Canc Res Ctr, Mol Targets Drug Discovery Program, Frederick, MD 21702 USA
    1. Year: 2002
  2. Journal: Protein Expression and Purification
    1. 26
    2. 1
    3. Pages: 42-49
  4. Type of Article: Article
  1. Abstract:

    Cyanovirin-N (CV-N) is under development as a topical (vaginal or rectal) microbicide to prevent sexual transmission of human immunodeficiency virus (HIV), and an economically feasible means for very large-scale production of tile protein is all urgent priority. We observed that N-glycosylation of CV-N in yeast eliminated the anti-HIV activity, and that dimeric forms and aggregates of CV-N occurred under certain conditions, potentially complicating the efficient large-scale manufacture of pure monomeric CV-N. We therefore expressed and tested CV-N homologs in which tile Asn residue ill position 30 was replaced with Ala, Gin, or Val, and/or the Pro at position 51 was replaced by Gly to eliminate potential conformational heterogeneity. All homologs exhibited anti-HIV activity comparable to wild-type CV-N. and the Pro51Gly homologs were significantly more stable proteins. These glycosylation- resistant, functional cyanovirins should he amenable to large- scale production either in bacteria or in eukaryotic hosts. (C) 2002 Elsevier Science (USA). All rights reserved.

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