Document 0042
 DOCN  M9460042
 TI    Production of linear polymers of HIV gp120-binding domains [letter]
 DT    9408
 AU    Smythe JA; Nardelli B; Chatterjee P; Gallo RC; Gershoni JM
 SO    Protein Eng. 1994 Feb;7(2):145-7. Unique Identifier : AIDSLINE
       MED/94224745
 AB    It has been demonstrated previously that molecular decoys of the
       acetylcholine receptor have therapeutic efficacy as antitoxins
       [Gershoni, J. and Aronheim, A. (1988) Proc. Natl Acad. Sci. USA, 85,
       4087-4089], but surely a most challenging goal is to apply this approach
       towards the development of antiviral drugs. As viruses present multiple
       copies of their envelope proteins, it was proposed that polyvalent
       decoys could be advantageous. Here we report the design and expression
       of recombinant linear polymers of the HIV gp120-binding domains which
       are situated within the T-cell membrane protein CD4. Whereas the
       production of linear concatemers of CD4 variable domains is feasible, a
       number of conformational constraints must be considered when designing a
       polymeric molecule which retains biological function. Most significant
       is the contribution of domains flanking the binding site that apparently
       enable correct folding of the latter.
 DE    Antigens, CD4/*METABOLISM  Antiviral Agents/CHEMISTRY/*METABOLISM  HIV
       Envelope Protein gp120/*METABOLISM  Plasmids  Polymers  Protein Binding
       *Protein Engineering  Recombinant Fusion Proteins/*METABOLISM  LETTER
       JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).