Document 1017
 DOCN  M9541017
 TI    Monoclonal antibodies against HIV type 1 integrase: clues to molecular
       structure.
 DT    9504
 AU    Bizub-Bender D; Kulkosky J; Skalka AM; Fox Chase Cancer Center,
       Institute for Cancer Research,; Philadelphia, Pennsylvania 19111.
 SO    AIDS Res Hum Retroviruses. 1994 Sep;10(9):1105-15. Unique Identifier :
       AIDSLINE MED/95127293
 AB    Eleven murine hybridoma clones were selected for their ability to
       produce anti-HIV-1 integrase (IN) antibodies. Competition and epitope
       mapping studies allowed segregation of the monoclonal antibodies (MAbs)
       into four distinct classes. The five MAbs that comprise the first class
       showed high affinity for epitopes within an N-terminal domain of 58
       amino acids that includes a conserved zinc finger motif. The second
       class, with two MAbs, showed high affinity for epitopes within 29 amino
       acids at the C terminus. Another two MAbs, which constitute the third
       class, displayed moderate affinities for epitopes that mapped to regions
       within the highly conserved catalytic core referred to as the D,D(35)E
       domain. One of these MAbs showed significant cross-reactivity with HIV-2
       IN and weak, but detectable, cross-reactivity with RSV IN. The remaining
       two MAbs, which comprise the fourth class, exhibited fairly low binding
       affinities and appeared to recognize epitopes in the zinc finger motif
       domain as well as the C-terminal half of the IN protein. The MAbs can be
       used for immunoprecipitation and immunoblotting procedures as well as
       for purification of HIV-1 IN protein by affinity chromatography. We show
       that several can also be used to immunostain viral IN sequences in
       HIV-1-infected T cells, presumably as a component of Gag-Pol precursors.
       Finally, analysis of our mapping and competition data suggests a
       structure for mature IN in which the C terminus approaches the central
       core domain, and the N and C termini touch or are proximal to each
       other. These MAbs should prove useful for further analyses of the
       structure and function of IN both in vitro and in vivo.
 DE    Amino Acid Sequence  Animal  *Antibodies,
       Monoclonal/CLASSIFICATION/ISOLATION & PURIF  Antigenic
       Determinants/ANALYSIS  Chimeric Proteins/ANALYSIS/IMMUNOLOGY
       Comparative Study  Conserved Sequence  Cross Reactions  DNA
       Nucleotidyltransferases/*ANALYSIS/*IMMUNOLOGY  Enzyme-Linked
       Immunosorbent Assay  Female  Hybridomas  HIV-1/*ENZYMOLOGY/GENETICS
       HIV-2/ENZYMOLOGY  IgG/CLASSIFICATION/ISOLATION & PURIF  Immunoblotting
       Mice  Mice, Inbred BALB C/IMMUNOLOGY  Recombinant
       Proteins/ANALYSIS/IMMUNOLOGY  Sequence Deletion  Support, Non-U.S. Gov't
       Support, U.S. Gov't, Non-P.H.S.  Support, U.S. Gov't, P.H.S.
       T-Lymphocytes/IMMUNOLOGY/*VIROLOGY  Virus Integration  JOURNAL ARTICLE

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