Document 0339
 DOCN  M9610339
 TI    Enhancing the avidity of a human recombinant anti-HIV-1 monoclonal
       antibody through oligomerization.
 DT    9601
 AU    Tsai PK; Burke CJ; Irwin JW; Bruner MW; Tung JS; Hollis GF; Mark GE;
       Kessler JA 2nd; Boots LJ; Conley AJ; et al; Department of Pharmaceutical
       Research, Merck Research; Laboratories, West Point, PA 19486, USA.
 SO    J Pharm Sci. 1995 Jul;84(7):866-70. Unique Identifier : AIDSLINE
       MED/96057251
 AB    The oligomerization by chemical cross-linking of a recombinant human
       antiviral monoclonal antibody (MAb), r447-1, and its characterization
       are described. This MAb binds to an epitope residing in the
       hypervariable V3 region of the envelope protein (gp120/160) of HIV-1. A
       dimeric form of this MAb displays enhanced avidity and was found to be
       capable of neutralizing a greater variety of lymphoid cell
       culture-adapted HIV-1 variants and HIV-1 primary isolates than its
       monomeric form. The superior binding and breadth of reactivity of this
       antibody suggests it may have utility as a therapeutic and/or
       prophylactic agent, if it possesses an appropriate safety and
       immunogenicity profile.
 DE    Antibodies, Monoclonal/*GENETICS  Antigens/IMMUNOLOGY  Chromatography
       Human  HIV-1/*IMMUNOLOGY  Molecular Structure  Proteins/METABOLISM
       Recombination, Genetic  Time Factors  JOURNAL ARTICLE

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