Document 1075
 DOCN  M9591075
 TI    The HIV-1 V3 domain on field isolates: participation in generation of
       escape virus in vivo and accessibility to neutralizing antibodies.
 DT    9509
 AU    Arendrup M; Akerblom L; Heegaard PM; Nielsen JO; Hansen JE; Department
       of Infectious Diseases, University of Copenhagen,; Hvidovre Hospital,
       Denmark.
 SO    Arch Virol. 1995;140(4):655-70. Unique Identifier : AIDSLINE
       MED/95314457
 AB    The V3 domain is highly variable and induces HIV neutralizing antibodies
       (NA). Here we addressed the issues of 1) the participation of mutations
       in V3 in generation of neutralization resistant escape virus in vivo and
       2) the applicability of synthetic V3 peptides corresponding to field
       isolates to induce neutralizing immune sera. Seven peptides
       corresponding to the V3 region of primary and escape virus from 3 HIV-1
       infected patients were synthesized and used for antibody (Abs) studies
       and immunizations. The anti-V3 Abs titre in patient serum was generally
       low against peptides corresponding to autologous virus isolated later
       than the serum sample in contrast to the titre against peptides
       corresponding to virus isolated earlier than the serum sample.
       Furthermore, neutralizing anti-V3 monoclonal antibodies (MAbs) raised
       against V3 peptides from laboratory strains of HIV-1 showed distinct
       binding patterns against V3 peptides corresponding to sequential primary
       and escape field isolates, with the strongest reactivity against late
       isolated escape virus. These observations suggest that the
       neutralization epitope was influenced by the appearance of mutations.
       When used as immunogen in rabbits, V3 peptides corresponding to field
       isolates were highly immunogenic but failed to induce neutralizing or
       gp120-precipitating Abs. On the contrary, V3 peptide corresponding to
       the laboratory strain HXB2 induced HIV neutralizing, gp120-precipitating
       immune serum. In conclusion, these data suggest a participation of the
       V3 domain in the immunoselection of escape virus, and that V3 on early
       field virus is less accessible to NA than that on laboratory strains.
 DE    Amino Acid Sequence  Animal  Human  HIV Envelope Protein
       gp120/*IMMUNOLOGY  HIV-1/GENETICS/*IMMUNOLOGY/ISOLATION & PURIF  Immune
       Sera  Immunization  Molecular Sequence Data  Mutation  Neutralization
       Tests  Peptide Fragments/*IMMUNOLOGY  Rabbits  Support, Non-U.S. Gov't
       JOURNAL ARTICLE

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