Cross-reactivity of monoclonal antibodies to a chimeric V3 peptide of HIV-1 with peptide analogues studied by biosensor technology and ELISA

Richalet-Sécordel, Pascale M.; Zeder‐Lutz, Gabrielle; Plaué, S.; Sommermeyer-Leroux, Ghislaine; Regenmortel, M.H.V. Van

doi:10.1016/0022-1759(94)90316-6

Cited by 27 publications

(7 citation statements)

References 25 publications

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“…The usefulness of cyclization as a means to enhance the antigenicity of peptides that, in the linear form, do not suitably reproduce the antigenic behavior of the native antigen has been generally acknowledged [14,[29][30][31][32][33]. In this work, we have successfully applied the cyclization approach to the GH loop of FMDV C-S30 and found an improvement of two orders of magnitude in the recognition by mAb 4C4 relative to the linear form.…”

Section: Rele6ance Of Conformation In Linear Antigenic Sitesmentioning

confidence: 92%

Antigenicity modulation upon peptide cyclization: application to the GH loop of foot-and-mouth disease virus strain C1-Barcelona

Gomes

Giralt

Andreu

2001

Vaccine

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Foot-and-mouth disease virus (FMDV) isolate C 1 -Barcelona (or C-S30) includes four replacements within its immunodominant site (GH loop, residues 136-150 of capsid protein VP1, YTTSTRGDLAHVTAT), relative to reference strain C-S8c1 (YTASAR-GDLAHLTTT). Although one of the mutations in C-S30 ( 147 Leu Val) is known to be detrimental for antibody recognition, reactivity of this isolate with the neutralizing monoclonal antibody (mAb) 4C4, raised against FMDV C 1 -Brescia (GH loop: YTASTRGDLAHLTAT), was indistinguishable from those of strains C-S8c1 or C 1 -Brescia. A structural interpretation for these somewhat striking findings is available, based on the observation that 15-residue peptides reproducing the C-S30 and C-S8c1 GH loops adopt very similar, quasi-circular, conformations in crystal complexes with 4C4. Nevertheless, surface plasmon resonance (SPR) kinetic analyses of the interactions between these peptides and three anti-GH loop mAbs have now revealed that the linear C-S30 peptides were less antigenic in solution than their C-S8c1 and C 1 -Brescia counterparts. We have, therefore, tried to modulate peptide antigenicity in solution by cyclization. Functional SPR and structural two dimensional proton nuclear magnetic resonance (2D-1 H NMR) studies of both linear and cyclic peptide antigens are discussed here. Conformation seems to have an important role in peptide antigenicity, even when continuous (i.e. linear) antigenic sites are involved.

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Section: Rele6ance Of Conformation In Linear Antigenic Sitesmentioning

confidence: 92%

Antigenicity modulation upon peptide cyclization: application to the GH loop of foot-and-mouth disease virus strain C1-Barcelona

Gomes

Giralt

Andreu

2001

Vaccine

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“…Due to the structural insights gained thus far, it appears that immunogen design strategies that target V3 need to take into account V3 structure and not simply focus on sequence. Design strategies include stabilization of V3 peptides on protein scaffolds or chimeras [34,79,109,162,313], conformationally constraining V3 via mutagenesis or chemically [13,14,28,118,122,277,278,336,337], conjugation of V3 peptides to foreign or carrier proteins [59,64,65,154], and identifying V3 variants or consensus sequences representative of potential V3 structures [93,94,138,206,325].…”

Section: Targeting the Chemokine Receptor Bind-ing Sitementioning

confidence: 99%

Designing Immunogens to Elicit Broadly Neutralizing Antibodies to the HIV-1 Envelope Glycoprotein

Lin

Nara²

2007

CHR

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To date HIV-1 vaccines have not been able to elicit potent, long lasting, and broadly neutralizing antibodies to the virus. Our knowledge of HIV envelope glycoprotein (Env) structure/function and the existence of a handful of broadly neutralizing antibodies is guiding rational immunogen design. We review here the potential targets on the HIV Env (the glycan shield, the CD4 binding site, the coreceptor binding site, Env fusion intermediates, and the membrane proximal region) and their associated rational immunogen design strategies. Moreover, we discuss immune dampening and immune refocusing strategies designed to counter immunodominant, decoy responses generated by the virus. In this regard, an immunogen design strategy of "in vitro de-evolution" is presented, which begins to distill the HIV Env to its most critical, core functional domains. While we are beginning to have some understanding as to where we would like out immune system to go, we find that our immune repertoire may actually have limits that preclude successful completion of the task at hand. The repertoire limits appear to be a byproduct of autoantibody tolerance mechanisms and the complex structural requirements for effective, potent broadly neutralizing antibodies. Nevertheless, the hope is that through novel insights and creative solutions that we will be able to design immunogens capable of eliciting broadly neutralizing antibodies to the HIV envelope glycoprotein.

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“…(13,14) Controlled surface immobilisation by thiol coupling was used to control dimerisation of the extracellular domain of the human growth hormone receptor immobilised on the sensor surface. (13) Affinity-capture techniques can be used after immobilisation of a suitable primary reagent, using NHS/EDC.…”

Section: Protein and Peptide Immobilisationmentioning

confidence: 99%

Instrumental biosensors: new perspectives for the analysis of biomolecular interactions

1999

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Cross-reactivity of monoclonal antibodies to a chimeric V3 peptide of HIV-1 with peptide analogues studied by biosensor technology and ELISA

Cited by 27 publications

References 25 publications

Antigenicity modulation upon peptide cyclization: application to the GH loop of foot-and-mouth disease virus strain C1-Barcelona

Antigenicity modulation upon peptide cyclization: application to the GH loop of foot-and-mouth disease virus strain C1-Barcelona

Designing Immunogens to Elicit Broadly Neutralizing Antibodies to the HIV-1 Envelope Glycoprotein

Instrumental biosensors: new perspectives for the analysis of biomolecular interactions

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