Fine specificity of the antibody response to a synthetic peptide from the fusion protein and protection against measles virus-induced encephalitis in a mouse model.

Partidos, Charalambos D.; Ripley, J.; Delmas, A.F.; Obeid, Obeid E.; Denbury, Andrew N.; Steward, M. W.

doi:10.1099/0022-1317-78-12-3227

Cited by 19 publications

(9 citation statements)

References 17 publications

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“…20 -21 MEAL comprises a linear epitope of 11 residues from the F protein of Measles Virus (MV). 22 OMP31 peptide comprises a sequence included in an exposed loop of the Outer Membrane Protein OMP31 of Brucella melitensis. 23…”

Section: Origin Of the Inserted Peptidesmentioning

confidence: 99%

Engineering of a polymeric bacterial protein as a scaffold for the multiple display of peptides

et al. 2004

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Protein assemblies with a high degree of repetitiveness and organization are known to induce strong immune responses. For that reason they have been postulated for the design of subunit vaccines by means of protein engineering. The enzyme lumazine synthase from Brucella spp. (BLS) is highly immunogenic, presumably owing to its homodecameric arrangement and remarkable thermodynamic stability. Structural analysis has shown that it is possible to insert foreign peptides at the ten amino terminus of BLS without disrupting its general folding. These peptides would be displayed to the immune system in a highly symmetric three-dimensional array. In the present work, BLS has been used as a protein carrier of foreign peptides. We have established a modular system to produce chimeric proteins decorated with ten copies of a desired peptide as long as 27 residues and have shown that their folding and stability is similar to that of the wild-type protein. The knowledge about the mechanisms of dissociation and unfolding of BLS allowed the engineering of polyvalent chimeras displaying different predefined peptides on the same molecular scaffold. Moreover, the reassembly of mixtures of chimeras at different steps of the unfolding process was used to control the stoichiometry and spatial arrangement for the simultaneous display of different peptides on BLS. This strategy would be useful for vaccine development and other biomedical applications.

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Section: Origin Of the Inserted Peptidesmentioning

confidence: 99%

Engineering of a polymeric bacterial protein as a scaffold for the multiple display of peptides

et al. 2004

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“…It would be interesting to see if this also holds in a broader comparison with immunization in other common hosts such as rat, mouse or goat. Earlier studies with peptide immunizations in mice have shown similar results where the epitope region of the antibodies shifts in length and direction [27].…”

Section: Discussionmentioning

confidence: 53%

Parallel Immunizations of Rabbits Using the Same Antigen Yield Antibodies with Similar, but Not Identical, Epitopes

et al. 2012

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A problem for the generation of polyclonal antibodies is the potential difficulties for obtaining a renewable resource due to batch-to-batch variations when the same antigen is immunized into several separate animals. Here, we have investigated this issue by determining the epitopes of antibodies generated from parallel immunizations of rabbits with recombinant antigens corresponding to ten human protein targets. The epitopes were mapped by both a suspension bead array approach using overlapping synthetic 15-mer peptides and a bacterial display approach using expression of random fragments of the antigen on the surface of bacteria. Both methods determined antibody binding with the aid of fluorescent-based analysis. In addition, one polyclonal antibody was fractionated by peptide-specific affinity capture for in-depth comparison of epitopes. The results show that the same antigen immunized in several rabbits yields polyclonal antibodies with similar epitopes, but with larger differences in the relative amounts of antibodies to the different epitopes. In some cases, unique epitopes were observed for one of the immunizations. The results suggest that polyclonal antibodies generated by repeated immunizations do not display an identical epitope pattern, although many of the epitopes are similar.

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“…Peptides with contiguous B‐ and T epitopes have been reported to give a protective immune response in the absence of carrier molecules (42–45). However, little is known about the immunogenicity of glycopeptides as far as antibody production against the sugar moiety is concerned.…”

Section: Resultsmentioning

confidence: 99%

Short synthetic glycopeptides successfully induce antibody responses to carcinoma‐associated Tn antigen

Vichier-Guerre¹,

Lo‐Man²,

Bay³

et al. 2000

The Journal of Peptide Research

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Glycopeptides containing a tumor-associated carbohydrate antigen (mono-, tri- or hexa-Tn antigen) as a B-cell epitope and a CD4+ T-cell epitope (PV: poliovirus or TT: tetanus toxin) were prepared for immunological studies. Several Tn antigen residues [FmocSer/Thr (alpha-GalNAc)-OH] were successively incorporated into the peptide sequence with unprotected carbohydrate groups. The tri- and hexa-Tn glycopeptides were recognized by MLS128, a Tn-specific monoclonal antibody. The position of the tri-Tn motif in the peptide sequence and the peptide backbone itself do not alter its antigenicity. As demonstrated by both ELISA and FACS analysis, the glycopeptides induced high titers of anti-Tn antibodies in mice, in the absence of a carrier molecule. In addition, the generated antibodies recognized the native Tn antigen on cancer cells. The antibody response obtained with a D-(Tn3)-PV glycopeptide containing three alpha-GalNAc-D-serine residues is similar that obtained with the Tn6-PV glycopeptide. These results demonstrate that short synthetic glycopeptides are able to induce anticancer antibody responses.

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Fine specificity of the antibody response to a synthetic peptide from the fusion protein and protection against measles virus-induced encephalitis in a mouse model.

Cited by 19 publications

References 17 publications

Engineering of a polymeric bacterial protein as a scaffold for the multiple display of peptides

Engineering of a polymeric bacterial protein as a scaffold for the multiple display of peptides

Parallel Immunizations of Rabbits Using the Same Antigen Yield Antibodies with Similar, but Not Identical, Epitopes

Short synthetic glycopeptides successfully induce antibody responses to carcinoma‐associated Tn antigen

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