1997
DOI: 10.1016/s0092-8674(00)80468-7
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Molecular Basis for the Binding Promiscuity of an Anti-p24 (HIV-1) Monoclonal Antibody

Abstract: Multiple binding capabilities utilized by specific protein-to-protein interactions in molecular recognition events are being documented increasingly but remain poorly understood at the molecular level. We identified five unrelated peptides that compete with each other for binding to the paratope region of the monoclonal anti-p24 (HIV-1) antibody CB4-1 by using a synthetic positional scanning combinatorial library XXXX[B1,B2,B3,X1,X2,X3]XXXX (14 mers; 68,590 peptide mixtures in total) prepared by spot synthesis… Show more

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Cited by 187 publications
(148 citation statements)
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“…17 In these studies, one monoclonal antibody was found to bind a set of non-homologous peptides, but the peptides adopted different binding conformations and formed their critical interaction with different antibody residues. 19,20 This might indicate that structurally different (peptide) binding motifs could be obtained for any monoclonal antibody, 19 which if established, would impact, for example the way we search for auto-antigens and design peptide motifs for immunization. In the other example, a set of peptides were observed to adopt spatially different footprints within the antigen-combining site of the antibody, but they shared a conformation-specific lock involving two residues on the antibody.…”
Section: Discussionmentioning
confidence: 99%
See 2 more Smart Citations
“…17 In these studies, one monoclonal antibody was found to bind a set of non-homologous peptides, but the peptides adopted different binding conformations and formed their critical interaction with different antibody residues. 19,20 This might indicate that structurally different (peptide) binding motifs could be obtained for any monoclonal antibody, 19 which if established, would impact, for example the way we search for auto-antigens and design peptide motifs for immunization. In the other example, a set of peptides were observed to adopt spatially different footprints within the antigen-combining site of the antibody, but they shared a conformation-specific lock involving two residues on the antibody.…”
Section: Discussionmentioning
confidence: 99%
“…The set of tryptic peptides bound by each individual CIMS antibody was thus detected and identified using tandem-mass spectrometry. The results showed that peptides of a median length of 10 amino acids (range [6][7][8][9][10][11][12][13][14][15][16][17][18][19][20][21][22] and with a median pI of 6.5 (range 3.8-12) were captured in a clone-dependent manner (Table I). Noteworthy, as illustrated for the CIMS-17 sister pair, the affinity (K D ) for an experimentally verified captured yeast peptide was found to be in the same range as that observed for the original selection peptide (Table I).…”
Section: Degenerate Peptide-binding Specificitymentioning
confidence: 99%
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“…To identify these sites, we screened cellulose-bound peptide libraries representing the complete sequences of ␥C and ␤C for ␣ M I-domain binding. Previously, cellulose-bound peptide libraries were widely utilized to define the mechanisms of recognition in biological systems in which promiscuity in ligand binding plays an important role (12)(13)(14). We found that the ␣ M I-domain bound to many short linear sequences scattered throughout the ␥C and ␤C structural domains.…”
mentioning
confidence: 94%
“…4 Different mechanisms have been proposed to explain it, including the existence of several isoforms with distinct recognition profile 5 or the use of different sets of residues of the binding site. 6 Multispecificity characterizes a major fraction of the antibodies of the natural repertoire, which recognize a collection of autologous and heterologous molecules. 7,8 Nevertheless, some antibodies resulting from antigen-driven selection have been shown to be polyreactive.…”
Section: Introductionmentioning
confidence: 99%