Document 0735
 DOCN  M9650735
 TI    Antigenic analysis of HIV type 1 external envelope (Env) glycoprotein C2
       region: implication for the structure of Env.
 DT    9605
 AU    Lemasson I; Housset V; Calas B; Devaux C; Laboratoire d'Immunologie des
       Infections Retrovirales, CNRS; UPR9008 et INSERM U249, Montpellier,
       France.
 SO    AIDS Res Hum Retroviruses. 1995 Oct;11(10):1177-86. Unique Identifier :
       AIDSLINE MED/96157205
 AB    To determine whether the amino acid sequence extending from residue 273
       to residue 288 in the second conserved region C2 of the HIV-1 envelope
       glycoprotein represents a target for antibodies on monomeric and
       oligomerized HIV-1 gp120env, we characterized several antisera and
       monoclonal antibodies (MAb) raised against C2 synthetic peptides. A
       cross-reactive epitope was evidenced on HIV-1Lai and HIV-1Eli C2-derived
       peptides, but was not encountered on HIV-2 C2-derived peptide. This
       epitope was found to be expressed on the native monomeric gp120env but
       was not detected in the context of oligomeric Env, suggesting this
       region is sequestered in the oligomeric molecule. Preincubation of
       oligomeric Env with sCD4 apparently failed to expose this epitope. Our
       results suggest that the amino acid sequence extending from residue 273
       to residue 288 in C2 of HIV-1 gp120env may be involved in intermolecular
       interaction within the oligomeric Env complex.
 DE    Amino Acid Sequence  Animal  Antibodies, Monoclonal/IMMUNOLOGY  Cell
       Line  Female  Human  HIV Antibodies/IMMUNOLOGY  HIV
       Antigens/*CHEMISTRY/IMMUNOLOGY  HIV Envelope Protein
       gp120/*CHEMISTRY/IMMUNOLOGY  HIV-1/*CHEMISTRY/IMMUNOLOGY  Mice  Mice,
       Inbred BALB C  Molecular Sequence Data  Protein Conformation  Support,
       Non-U.S. Gov't  JOURNAL ARTICLE

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