Antigenic cross-reactivity potential of synthetic peptides immobilized on polyethylene rods

Trifilieff, Élisabeth; Dubs, M.C.; Regenmortel, M.H.V. Van

doi:10.1016/0161-5890(91)90053-m

Cited by 50 publications

(14 citation statements)

References 31 publications

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“…Although a subpopulation of reactive antibodies could be binding to linear epitopes present on a few peptides (particularly peptides 45-64, 95-114, 115-134, and 275-294, which were recognized in a genetically unrestricted manner), these peptides may have a high conformational stability, particularly when attached to a plastic ELISA plate. This is similar to the stabilization of a folded structure when peptides are resin bound (15,34), attached to polyethylene pins (36,45), or conjugated to a carrier protein (8,9). Previous studies using monoclonal antibodies generated against native OmpF trimers and denatured monomers have shown that, in almost all cases, antibodies which were generated against the native protein reacted weakly or were negative when tested against a denatured monomer (24, 55), indicating that these antibodies were also conformation dependent.…”

Section: Discussionmentioning

confidence: 78%

Identification of Murine B-Cell and T-Cell Epitopes ofEscherichia coliOuter Membrane Protein F with Synthetic Polypeptides

2000

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Section: Discussionmentioning

confidence: 78%

Identification of Murine B-Cell and T-Cell Epitopes ofEscherichia coliOuter Membrane Protein F with Synthetic Polypeptides

2000

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“…It was observed that some peptides including only framework residues do specifically bind to the antigen; this is possibly due in certain cases to occurrence in the framework sequence of similarities with the motifs contributing to antigen binding. It has been shown that a sequence homology of three residues in a peptide is sufficient to give rise to antigenic cross-reactivity (30). However, in several instances there is no obvious homology so that the chemical or structural basis for this reactivity remains to be assessed.…”

Section: Discussionmentioning

confidence: 99%

“…For the L3 region, the 91 WGR-P 96 residues of the antigen-antibody complex were identified by peptide analysis with, however, the implication of an additional residue (Phe 98 ). For the H1 region, four CDR residues (DYW-E) and one framework residue (Ser 30 ) were found by crystallography to be implicated in antigen recognition; by alanine scanning of hexapeptides, the same five amino acids, 30 SDYW-E 35 , were found to be contributors. However, three other amino acids (Y-F------W) outside the CDR seemed to be implicated in the interaction of the peptide with the antigen.…”

Section: Antigen-binding Peptides From Antibody Variable Regionsmentioning

confidence: 99%

Systematic Exploration of the Antigen Binding Activity of Synthetic Peptides Isolated from the Variable Regions of Immunoglobulins

Laune

Molina

Ferrières

et al. 1997

Journal of Biological Chemistry

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Sets of short (12 residues) cellulose-bound synthetic overlapping peptides derived from the sequences of the variable regions of the heavy and light chains of three different antibodies (an anti-thyroglobulin antibody, the HyHEL-5 anti-lysozyme antibody, and an anti-angiotensin II antibody) were used to systematically assess the antigen binding capacity of peptides from the antibody paratope outside their natural molecular context. Peptides enclosing one or several of the complementarity determining region (CDR) residues had antigen binding activity, although the most active peptides were not necessarily those bearing the greatest number of CDR residues. Several residues from the framework region, preceding or following the CDR, were found to play a role in binding. Affinity constants from 4.1 ؋ 10 ؊7 to 6.7 ؋ 10 ؊8 M ؊1 for the soluble form of 9 lysozymebinding dodecapeptides were measured by BIAcore analysis. Alanine scanning of lysozyme-binding hexapeptides from the HyHEL-5 sequence identified 38 residues important for binding, of which 22 corresponded to residues that had been shown by x-ray crystallography to be at the interface between HyHEL-5 and lysozyme. Our results could be of interest for the rational identification of biologically active peptides derived from antibody sequences and in providing an experimental basis for mutagenesis of the antibody paratope.Antibody molecules bind antigens with high affinity and specificity by synergistically using multiple noncovalent forces. The combining site (paratope), whose shape is complementary to the epitope on the antigen, is made up of the hypervariable regions, also called complementarity determining regions (CDRs) 1 (1). It is commonly accepted that there are three CDRs in the light chain (L1, L2, and L3) and in the heavy chain (H1, H2, and H3). These CDRs fold into turn structures that are stabilized by the ␤-sheet framework of the variable domains. The interface between antibodies and antigens has been precisely described by x-ray crystallographic studies, and several complexes between Fab fragments of monoclonal antibodies and peptide or protein antigens have been recently described (for reviews see Refs. 2-4). The structures of antibody-antigen complexes indicate that at least four of the CDRs, and in some cases all six CDRs, contribute to antigen binding (5). Residues in the framework have rarely been reported to participate in this interaction (6, 7).Antibody-peptide or antibody-protein complexes are excellent model systems to study the physicochemical requirements for molecular recognition. Unfortunately, it is a difficult task to obtain crystals suitable for the structural elucidation of antibody fragments in complex with proteins or peptides. Therefore, other approaches to obtain information about the key residues involved in the interaction would be very useful, in particular for paratope mutagenesis. Some workers have demonstrated that synthetic peptides derived from the amino acid sequences of CDRs bind antigens with specificities similar to t...

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“…The three anti-cryptotope MAbs (57, 161 shown in Fig. 3; 174 data not shown) that inhibited translation have been shown to recognize amino acids 139 to 144, 90 to 98 and 140 to 145 of TMV coat protein respectively (A1 Moudallal et al, 1985;Trifilieff et al, 1991). The region 139 to 150 corresponds to the connection of a-helix LR with the C terminus of the polypeptide chain, whereas the region 90 to 98 connects the a-helix RR to the top of the set of reverse turns facing the central hole (Namba et al, 1989).…”

Section: S H O R T C O M M U N I C a T I O Nmentioning

confidence: 99%

Inhibition of in vitro Cotranslational Disassembly of Tobacco Mosaic Virus by Monoclonal Antibodies to the Viral Coat Protein

Saunal

Witz

Regenmortel

1993

Journal of General Virology

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It has been shown by others that translation of tobacco mosaic virus (TMV) RNA may begin before uncoating of particles is complete.We provide evidence that this cotranslational disassembly can be inhibited by incubating TMV treated at pH 8 with certain monoelonal antibodies (MAbs) specific for TMV coat protein.The most efficient inhibition was achieved by incubation with some anti-metatope MAbs known to bind to the TMV extremity that becomes disassembled first and contains the 5" end of the RNA, as well as with some anti-cryptotope MAbs that bind only to dissociated coat protein subunits.

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Antigenic cross-reactivity potential of synthetic peptides immobilized on polyethylene rods

Cited by 50 publications

References 31 publications

Identification of Murine B-Cell and T-Cell Epitopes ofEscherichia coliOuter Membrane Protein F with Synthetic Polypeptides

Identification of Murine B-Cell and T-Cell Epitopes ofEscherichia coliOuter Membrane Protein F with Synthetic Polypeptides

Systematic Exploration of the Antigen Binding Activity of Synthetic Peptides Isolated from the Variable Regions of Immunoglobulins

Inhibition of in vitro Cotranslational Disassembly of Tobacco Mosaic Virus by Monoclonal Antibodies to the Viral Coat Protein

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