Statistical Analysis and Tokenization of Epitopes to Construct Artificial Neoepitope Libraries 1 [Dataset]

Epitopes are specific regions on an antigen’s surface that the immune system recognizes. Epitopes are usually protein regions on foreign immune-stimulating entities such as viruses and bacteria, and in some cases, endogenous proteins may act as antigens. Identifying epitopes is crucial for accelerat...

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Detalles Bibliográficos
Autores: López-Martínez, Elena, Manteca, Aitor, Ferruz, Noelia, Cortajarena, Aitziber L.
Tipo de recurso: conjunto de datos
Estado:Versión publicada
Fecha de publicación:2023
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/356798
Acceso en línea:http://hdl.handle.net/10261/356798
Access Level:acceso abierto
Palabra clave:Universal epitope libraries
Natural language processing
Linear epitope libraries
Amino acid frequency
7 amino acids
Immune system recognizes
Immune epitope database
Usually protein regions
Conventional sequence analysis
Linear epitopes deposited
Foreign immune
Statistical analysis
Specific regions
Stimulating entities
Practically null
Pathogen proteomes
Methods inspired
Mapping epitopes
Identifying epitopes
Human proteome
Building blocks
Aromatic residues
Antigen ’
Descripción
Sumario:Epitopes are specific regions on an antigen’s surface that the immune system recognizes. Epitopes are usually protein regions on foreign immune-stimulating entities such as viruses and bacteria, and in some cases, endogenous proteins may act as antigens. Identifying epitopes is crucial for accelerating the development of vaccines and immunotherapies. However, mapping epitopes in pathogen proteomes is challenging using conventional methods. Screening artificial neoepitope libraries against antibodies can overcome this issue. Here, we applied conventional sequence analysis and methods inspired in natural language processing to reveal specific sequence patterns in the linear epitopes deposited in the Immune Epitope Database (www.iedb.org) that can serve as building blocks for the design of universal epitope libraries. Our results reveal that amino acid frequency in annotated linear epitopes differs from that in the human proteome. Aromatic residues are overrepresented, while the presence of cysteines is practically null in epitopes. Byte pair encoding tokenization shows high frequencies of tryptophan in tokens of 5, 6, and 7 amino acids, corroborating the findings of the conventional sequence analysis. These results can be applied to reduce the diversity of linear epitope libraries by orders of magnitude.