1989
DOI: 10.1099/0022-1317-70-6-1505
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Specificity and Function of the Individual Amino Acids of an Important Determinant of Human Immunodeficiency Virus Type 1 that Induces Neutralizing Activity

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Cited by 78 publications
(30 citation statements)
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“…Small peptides are sufficient to induce neutralizing antibodies [7,13,14,23]. This sequence contains a potential, in various virus isolates highly conserved [3-turn motif (GPGR) [ 19,15]. Flanking residues seem to be critical for antibody binding, virus type specific neutralization, inhibition of syncytia formation and stabilization of the structure of the V3-1oop.…”
Section: Introductionmentioning
confidence: 99%
“…Small peptides are sufficient to induce neutralizing antibodies [7,13,14,23]. This sequence contains a potential, in various virus isolates highly conserved [3-turn motif (GPGR) [ 19,15]. Flanking residues seem to be critical for antibody binding, virus type specific neutralization, inhibition of syncytia formation and stabilization of the structure of the V3-1oop.…”
Section: Introductionmentioning
confidence: 99%
“…Two separate, putative cysteine loops within the nine disulphide bonds reported for the molecule (Fennie & Lasky, 1989) contain the CD4-binding region (Lasky et al, 1987), by which the virus binds to its cellular receptor, and the immunodominant neutralizing epitope (Javaherian et al, 1989;Meloen et al, 1989).…”
Section: Introductionmentioning
confidence: 99%
“…Neutralization epitopes that are accessible on laboratoryadapted HIV-1 strains but are poorly represented on primary isolates include the V3 region (16,27,38), the CD4 binding site (19,21,29,33,48,49), and the V2 region (13,26,47) of gp120. The V3 loop, a disulfide cross-bridged loop in the third variable domain of gp120, has been described as the principal neutralization determinant for laboratory-adapted HIV-1 strains, such as HIV-1 LAI.…”
mentioning
confidence: 99%