Document 0503
 DOCN  M9480503
 TI    Differential regulation of cellular tropism and sensitivity to soluble
       CD4 neutralization by the envelope gp120 of human immunodeficiency virus
       type 1.
 DT    9410
 AU    Stamatatos L; Werner A; Cheng-Mayer C; Cancer Research Institute, School
       of Medicine, University of; California, San Francisco 94143-0128.
 SO    J Virol. 1994 Aug;68(8):4973-9. Unique Identifier : AIDSLINE
       MED/94309161
 AB    Using recombinant and mutant viruses generated between two human
       immunodeficiency virus type 1 isolates that display differences in cell
       tropism and sensitivity to soluble CD4 neutralization, we show that
       these two properties of the virus are regulated by different mechanisms.
       Whereas there is an association between V3 loop conformation and a
       particular cellular tropism, soluble CD4 neutralization sensitivity
       appears to be determined by amino acid differences in the C2 domain of
       the envelope gp120 that modulate the stability of gp120-gp41
       association. Our findings further illustrate the importance of
       functional interactions among different regions of the envelope gp120 in
       regulating the biological phenotypes of human immunodeficiency virus and
       suggest that additional probing of the V3 loop with monoclonal
       antibodies may identify specific structural features of this loop that
       determine cell tropism.
 DE    Amino Acid Sequence  Animal  Antibodies, Monoclonal/IMMUNOLOGY
       Antigens, CD4/*PHARMACOLOGY  Cell Line  Human  HIV Envelope Protein
       gp120/CHEMISTRY/*PHYSIOLOGY  HIV Envelope Protein gp41/PHYSIOLOGY
       HIV-1/IMMUNOLOGY/*PHYSIOLOGY  Molecular Sequence Data  Neutralization
       Tests  Peptide Fragments/CHEMISTRY/*PHYSIOLOGY  Phenotype  Protein
       Conformation  Solubility  Support, U.S. Gov't, P.H.S.  Transfection
       JOURNAL ARTICLE

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       protected by Copyright Law (Title 17, U.S.Code).