A cluster of continuous antigenic structures in the transmembrane protein of HIV-1: Individual patterns of reactivity in human sera Academic Article Article uri icon


MeSH Major

  • Antibodies, Neutralizing
  • HIV Antibodies
  • HIV Envelope Protein gp120


  • We investigated the antigenicity of a highly conserved region in the transmembrane protein of the human immunodeficiency virus type 1 (HIV-1). In order to identify antigenically important residues, amino-acid sequences of synthetic peptides representing this region were varied systematically: single residues were omitted from the sequence of HIV-env 583-599; threonines were substituted for pairs of residues in HIV-env 581-599; the sequences of heptadeca-peptides were shifted by single residues. The peptides were tested in an enzyme immuno-assay against fourteen HIV-1 antibody-positive human sera, which were previously found to react with HIV-env 583-599, and against rabbit antisera to the peptides HIV-env 583-599 and 586-606. Substitutions as well as deletions in the sequence 589-596 (AVERYLKD) aborgated the antigenicity of the peptides with most of the human sera. Changes outside this sequence affected the reactivities differentially. Six overlapping dodeca-peptides, shifted in the sequence by single residues, lacked antigenicity in a competition assay, suggesting antigenic dependence on an ordered peptide conformation, which the longer peptides may preferentially assume. 19- and 21-mers with overlapping sequences competed to different extents with each other for binding to the antibodies of 3 human sera, illustrating that more than one antigenic structure in this narrow region can be recognized by a single polyclonal serum.

publication date

  • January 1991



  • Academic Article


Digital Object Identifier (DOI)

  • 10.1016/0161-5890(91)90130-C

PubMed ID

  • 1713646

Additional Document Info

start page

  • 613

end page

  • 22


  • 28


  • 6