CD20-Mimotope Peptides: A Model to Define the Molecular Basis of Epitope Spreading
Antigen-mimicking peptide (mimotope)-based vaccines are one of the most promising forms of active-immunotherapy. The main drawback of this approach is that it induces antibodies that react poorly with the nominal antigen. The aim of this study was to investigate the molecular basis underlying the we...
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| Format: | Article |
| Language: | English |
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MDPI AG
2019-04-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/20/8/1920 |
| _version_ | 1811280701480239104 |
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| author | Elvira Favoino Marcella Prete Giacomo Catacchio Giuseppina Conteduca Federico Perosa |
| author_facet | Elvira Favoino Marcella Prete Giacomo Catacchio Giuseppina Conteduca Federico Perosa |
| author_sort | Elvira Favoino |
| collection | DOAJ |
| description | Antigen-mimicking peptide (mimotope)-based vaccines are one of the most promising forms of active-immunotherapy. The main drawback of this approach is that it induces antibodies that react poorly with the nominal antigen. The aim of this study was to investigate the molecular basis underlying the weak antibody response induced against the naïve protein after peptide vaccination. For this purpose, we analyzed the fine specificity of monoclonal antibodies (mAb) elicited with a 13-mer linear peptide, complementary to theantigen-combining site of the anti-CD20 mAb, Rituximab, in BALB/c mice. Anti-peptide mAb competed with Rituximab for peptide binding. Even so, they recognized a different antigenic motif from the one recognized by Rituximab. This explains their lack of reactivity with membrane (naïve) CD20. These data indicate that even on a short peptide the immunogenic and antigenic motifs may be different. These findings highlight an additional mechanism for epitope spreading and should be taken into account when designing peptides for vaccine purposes. |
| first_indexed | 2024-04-13T01:19:31Z |
| format | Article |
| id | doaj.art-0c7f0573197a4c7d90fdf25b1eb82bdd |
| institution | Directory Open Access Journal |
| issn | 1422-0067 |
| language | English |
| last_indexed | 2024-04-13T01:19:31Z |
| publishDate | 2019-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-0c7f0573197a4c7d90fdf25b1eb82bdd2022-12-22T03:08:49ZengMDPI AGInternational Journal of Molecular Sciences1422-00672019-04-01208192010.3390/ijms20081920ijms20081920CD20-Mimotope Peptides: A Model to Define the Molecular Basis of Epitope SpreadingElvira Favoino0Marcella Prete1Giacomo Catacchio2Giuseppina Conteduca3Federico Perosa4Department of Biomedical Sciences and Human Oncology (DIMO), Rheumatologic and Systemic Autoimmune Diseases Unit, University of Bari Medical School, I-70124 Bari, ItalyDepartment of Biomedical Sciences and Human Oncology (DIMO), Rheumatologic and Systemic Autoimmune Diseases Unit, University of Bari Medical School, I-70124 Bari, ItalyDepartment of Biomedical Sciences and Human Oncology (DIMO), Rheumatologic and Systemic Autoimmune Diseases Unit, University of Bari Medical School, I-70124 Bari, ItalyDepartment of Biomedical Sciences and Human Oncology (DIMO), Rheumatologic and Systemic Autoimmune Diseases Unit, University of Bari Medical School, I-70124 Bari, ItalyDepartment of Biomedical Sciences and Human Oncology (DIMO), Rheumatologic and Systemic Autoimmune Diseases Unit, University of Bari Medical School, I-70124 Bari, ItalyAntigen-mimicking peptide (mimotope)-based vaccines are one of the most promising forms of active-immunotherapy. The main drawback of this approach is that it induces antibodies that react poorly with the nominal antigen. The aim of this study was to investigate the molecular basis underlying the weak antibody response induced against the naïve protein after peptide vaccination. For this purpose, we analyzed the fine specificity of monoclonal antibodies (mAb) elicited with a 13-mer linear peptide, complementary to theantigen-combining site of the anti-CD20 mAb, Rituximab, in BALB/c mice. Anti-peptide mAb competed with Rituximab for peptide binding. Even so, they recognized a different antigenic motif from the one recognized by Rituximab. This explains their lack of reactivity with membrane (naïve) CD20. These data indicate that even on a short peptide the immunogenic and antigenic motifs may be different. These findings highlight an additional mechanism for epitope spreading and should be taken into account when designing peptides for vaccine purposes.https://www.mdpi.com/1422-0067/20/8/1920mimotopepeptideactive immunotherapyantigenicityimmunogenicityepitope spreadingvaccineCD20Rituximab |
| spellingShingle | Elvira Favoino Marcella Prete Giacomo Catacchio Giuseppina Conteduca Federico Perosa CD20-Mimotope Peptides: A Model to Define the Molecular Basis of Epitope Spreading International Journal of Molecular Sciences mimotope peptide active immunotherapy antigenicity immunogenicity epitope spreading vaccine CD20 Rituximab |
| title | CD20-Mimotope Peptides: A Model to Define the Molecular Basis of Epitope Spreading |
| title_full | CD20-Mimotope Peptides: A Model to Define the Molecular Basis of Epitope Spreading |
| title_fullStr | CD20-Mimotope Peptides: A Model to Define the Molecular Basis of Epitope Spreading |
| title_full_unstemmed | CD20-Mimotope Peptides: A Model to Define the Molecular Basis of Epitope Spreading |
| title_short | CD20-Mimotope Peptides: A Model to Define the Molecular Basis of Epitope Spreading |
| title_sort | cd20 mimotope peptides a model to define the molecular basis of epitope spreading |
| topic | mimotope peptide active immunotherapy antigenicity immunogenicity epitope spreading vaccine CD20 Rituximab |
| url | https://www.mdpi.com/1422-0067/20/8/1920 |
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