       Document 0467
 DOCN  M9620467
 TI    Conformational changes between human immunodeficiency virus type 1
       nucleocapsid protein NCp7 and its precursor NCp15 as detected by
       anti-NCp7 monoclonal antibodies.
 DT    9602
 AU    Tanchou V; Delaunay T; Bodeus M; Roques B; Darlix JL; Benarous R;
       Signalisation, Inflammation et Transformation Cellulaire, U332; INSERM,
       Paris, France.
 SO    J Gen Virol. 1995 Oct;76 ( Pt 10):2457-66. Unique Identifier : AIDSLINE
       MED/96030855
 AB    The nucleocapsid protein NCp15 of human immunodeficiency virus type 1
       (HIV-1) is a small basic protein with two zinc fingers. It is required
       for virion morphogenesis and synthesis of proviral DNA. As the first
       step in our study of the structural domains involved in the various
       functions of this protein, 18 monoclonal antibodies (MAbs) were
       isolated. The epitopes of NCp7 recognized by the MAbs were mapped using
       synthetic peptides representing overlapping sequences and truncated
       forms of NCp7. These anti-NCp7 MAbs were investigated by ELISA and
       real-time biospecific interaction analysis (BIAcore). Five classes of
       anti-NCp7 MAbs were characterized. Three classes (14 MAbs) were directed
       against continuous epitopes, one in the N-terminal part, another next to
       the second zinc finger and the third in the C-terminal part of the
       protein. Two other classes comprised four MAbs reacting only with the
       entire NCp7 and not with any of the small overlapping peptides used,
       suggesting that these MAbs were directed against conformational
       epitopes. The anti-NCp7 MAbs directed against linear epitopes were able
       to react efficiently with both NCp7 and NCp15, the NCp7 precursor,
       whereas the anti-NCp7 MAbs directed against conformational epitopes did
       not react with NCp15. Interestingly, most of the anti-NCp7 MAbs directed
       against conformational epitopes were capable of inhibiting the tight
       interaction between NCp7 and the HIV-1 replication primer tRNA(Lys,3).
       In contrast, most of the MAbs directed against linear epitopes did not
       inhibit this interaction.
 DE    Amino Acid Sequence  Animal  *Antibodies, Monoclonal  Antigen-Antibody
       Reactions  Binding, Competitive  Biosensors
       Capsid/*CHEMISTRY/IMMUNOLOGY  Epitope Mapping  Female  Gene Products,
       gag/*CHEMISTRY/IMMUNOLOGY  Human  *HIV Antibodies  HIV-1/*IMMUNOLOGY
       Mice  Mice, Inbred BALB C  Molecular Sequence Data  Peptides/CHEMICAL
       SYNTHESIS  *Protein Conformation  Protein Precursors/CHEMISTRY  Rats
       RNA, Transfer, Lys/ANALYSIS  Support, Non-U.S. Gov't  Zinc
       Fingers/IMMUNOLOGY  JOURNAL ARTICLE

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

