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ABSTRACT: Epitope mapping of a monoclonal antibody directed against Neisserial Heparin Binding Antigen using next generation sequencing of antigen-specific libraries

PROVIDER: PRJEB12225 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	ERR1197520_1.fastq.gz	Fastqsanger.gz
	ERR1197520_2.fastq.gz	Fastqsanger.gz
	ERR1197519_1.fastq.gz	Fastqsanger.gz
	ERR1197519_2.fastq.gz	Fastqsanger.gz

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Epitope mapping of a monoclonal antibody directed against Neisserial Heparin Binding Antigen

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Project description:The aim of the study was to determine the epitope targeted by 31E10/E7 mouse monoclonal antibody (mAb) and the cross-reactivity to linear peptide epitopes of 10 different Neisserial Heparin Binding Antigen (NHBA) variants. mAb 31E10/E7 was diluted at 1:200 and incubated on a custom PepStar Peptide Microarray platform printed with 560 different peptides in three independent experiments.

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Project description:The identification of protective epitopes in bacterial pathogens using mass spectrometry proteomics is essential for advancing vaccine design, especially against the backdrop of increasing antibiotic resistance. Our study introduces an innovative strategy, leveraging multi-modal mass spectrometry techniques, to decode the interaction between a neutralizing monoclonal antibody (nAb) and the Streptolysin O (SLO) toxin from Streptococcus pyogenes. By integrating XL-MS, HDX-MS, and computational modeling, we successfully identified and characterized a conserved protective epitope within SLO, providing critical insights for vaccine development. Utilizing a novel nAb sequenced through de novo bottom-up shotgun MS, we explored its binding mechanism and interaction with the SLO antigen with structural proteomics such as XL-MS and HDX-MS. This study not only clarifies the conformational epitope structure but also illuminated the antibody's unique protective mechanism mode. The epitope's high conservation (near 100%) across various S. pyogenes strains underscores its potential as a universal target for vaccine strategies. Additionally, our approach overcomes traditional limitations in epitope mapping, showcasing the power of mass spectrometry in resolving challenging antibody-antigen interfaces. Our findings represent a significant leap in understanding bacterial pathogenesis and immune defense, laying the groundwork for designing next-generation vaccines. The data generated from this study can guide the development of targeted therapies and vaccines, offering new solutions to combat severe streptococcal infections.

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Epitope mapping of an anti-plasmodium pfMSP119 antibody by Intact Transition Epitope Mapping - Targeted High-Energy Rupture of Extracted Epitopes

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