       Document 0738
 DOCN  M9650738
 TI    Fine specificity of antibody recognition may predict amino acid
       substitution in the third variable region of gp120 during HIV type 1
       infection.
 DT    9605
 AU    Langedijk JP; Zwart G; Goudsmit J; Meloen RH; Institute for Animal
       Science and Health (ID-DLO), Lelystad, The; Netherlands.
 SO    AIDS Res Hum Retroviruses. 1995 Oct;11(10):1153-62. Unique Identifier :
       AIDSLINE MED/96157202
 AB    To investigate how human immunodeficiency virus type 1 (HIV-1) escapes
       from antibodies directed against the neutralization domain in the third
       variable region (V3) of gp120, we examined precisely which amino acid
       contributed to antibody binding. From six HIV-1-infected individuals,
       sequential sera were tested for antibody binding to individually
       designed peptide panels. Each individual panel contained all V3 domain
       sequences of cloned HIV-1 variants obtained at several time points from
       the studied individual. We showed that the V3 domain is a major site for
       escape of the humoral immune response. We showed antibody binding was
       reduced by certain mutations in the V3 domain and sometimes concerted
       mutations rendered very distinct antigenic variants. The position and
       the number of the mutations that occurred during infection corresponded
       with the position and number of amino acids in the V3 domain that were
       important for binding to anti-V3 antibodies in the early immune
       response. The specificity of the antibody binding hardly changed during
       infection. Although mutations at several positions of the V3 domain
       reduced antibody binding, the mutations were limited to certain
       positions, probably because the function of the region has to be
       maintained. The amino acids that were important for binding in
       combination with the preference for changes at certain positions
       predicted to some extent the mutations that occurred later during
       infection.
 DE    Amino Acid Sequence  *Antibody Specificity  Epitopes/IMMUNOLOGY  Human
       HIV Antibodies/*IMMUNOLOGY  HIV Envelope Protein
       gp120/CHEMISTRY/*IMMUNOLOGY  HIV Seropositivity/BLOOD/*IMMUNOLOGY
       HIV-1/*IMMUNOLOGY  Longitudinal Studies  Molecular Sequence Data
       Peptide Fragments/CHEMISTRY/*IMMUNOLOGY  Support, Non-U.S. Gov't
       JOURNAL ARTICLE

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

