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Construction and Enhanced Cytotoxicity of a

  1. Author:
    Mori, T.
    Shoemaker, R. H.
    McMahon, J. B.
    Gulakowski, R. J.
    Gustafson, K. R.
    Boyd, M. R.

  2. Author Address

    Boyd MR NCI LAB DRUG DISCOVERY RES & DEV DEV THERAPEUT PROGRAM DIV CANC TREATMENT DIAG & CTR BLDG 1052 FREDERICK, MD 21702 USA NCI LAB DRUG DISCOVERY RES & DEV DEV THERAPEUT PROGRAM DIV CANC TREATMENT DIAG & CTR FREDERICK, MD 21702 USA
    1. Year: 1997
  2. Journal: Biochemical and Biophysical Research Communications
    1. 239
    2. 3
    3. Pages: 884-888
  4. Type of Article: Article
  1. Abstract:

    Cyanovirin-N (CV-N) is a novel 11-kDa anti-HIV(human immunodeficiency virus) protein that binds with high affinity to the viral envelope glycoprotein gp120, in contrast to soluble CD4 and most known neutralizing antibodies that bind gp120, CV-N exerts potent anti-viral activity against primary clinical HN isolates as well as laboratory-adapted strains of HIV. Here we describe the recombinant production, purification, and characterization of a chimeric toxin molecule, FLAG-CV-N-PE38, that contains CV-N as a gp120-targeting moiety linked to the translocation and cytotoxic domains of Pseudomonas exotoxin A. FLAG-CV-N-PE38 showed enhanced cytotoxicity to HIV-infected, gp120-expressing H9 cells compared to uninfected H9 cells. Competition experiments with free CV-N provided further support that the enhanced FLAG-CV-N-PE38-induced cytotoxicity was due to interactions of the CV-N moiety with cell surface gp120. This study establishes the feasibility of use of CV-N as a gp120-targeting sequence for construction and experimental therapeutic investigations of unique new chimeric toxins designed to selectively destroy HIV-infected host cells. (C) 1997 Academic Press. [References: 34]

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