Open AccessPrincipal neutralizing domain of the human immunodeficiency virus type 1 envelope protein.
Author(s) -
Kashi Javaherian,
Alphonse J. Langlois,
Charlene McDanal,
Kerstin Ross,
Larry Eckler,
Cindy L. Jellis,
Albert T. Profy,
James R. Rusche,
D. P. Bolognesi,
Scott D. Putney
Publication year - 1989
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.86.17.6768
Subject(s) - neutralizing antibody , peptide sequence , antibody , virology , amino acid , peptide , biology , neutralization , virus , viral envelope , biochemistry , genetics , gene
The principal neutralizing determinant of human immunodeficiency virus type 1 (HIV-1) is located in the external envelope protein, gp120, and has previously been mapped to a 24-amino acid-long sequence (denoted RP135). We show here that deletion of this sequence renders the envelope unable to elicit neutralizing antibodies. In addition, using synthetic peptide fragments of RP135, we have mapped the neutralizing determinant to 8 amino acids and found that a peptide of this size elicits neutralizing antibodies. This sequence contains a central Gly-Pro-Gly that is generally conserved between different HIV-1 isolates and is flanked by amino acids that differ from isolate to isolate. Antibodies elicited by peptides from one isolate do not neutralize two different isolates, and a hybrid peptide, consisting of amino acid sequences from two isolates, elicits neutralizing antibodies to both isolates. By using a mixture of peptides of this domain or a mixture of such hybrid peptides the type-specificity of the neutralizing antibody response to this determinant can perhaps be overcome.