Immunopeptidomics of Salmonella enterica Serovar Typhimurium-Infected Pig Macrophages Genotyped for Class II Molecules

Salmonellosis is a zoonotic infection that has a major impact on human health; consuming contaminated pork products is the main source of such infection. Vaccination responses to classic vaccines have been unsatisfactory; that is why peptide subunit-based vaccines represent an excellent alternative....

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Autores: Celis-Giraldo, Carmen Teresa, Suárez, Carlos F., Agudelo, William, Ibarrola, Nieves, Dégano, Rosa M., Díaz, Jaime, Manzano Román, Raúl, Patarroyo, M. A.
Formato: artículo
Estado:Versión publicada
Fecha de publicación:2024
País:España
Recursos:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/381070
Acesso em linha:http://hdl.handle.net/10261/381070
Access Level:acceso abierto
Palavra-chave:Salmonella typhimurium
Immunopeptidomics
Peptide
Vaccine
Pig
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spelling Immunopeptidomics of Salmonella enterica Serovar Typhimurium-Infected Pig Macrophages Genotyped for Class II MoleculesCelis-Giraldo, Carmen TeresaSuárez, Carlos F.Agudelo, WilliamIbarrola, NievesDégano, Rosa M.Díaz, JaimeManzano Román, RaúlPatarroyo, M. A.Salmonella typhimuriumImmunopeptidomicsPeptideVaccinePigSalmonellosis is a zoonotic infection that has a major impact on human health; consuming contaminated pork products is the main source of such infection. Vaccination responses to classic vaccines have been unsatisfactory; that is why peptide subunit-based vaccines represent an excellent alternative. Immunopeptidomics was used in this study as a novel approach for identifying antigens coupled to major histocompatibility complex class II molecules. Three homozygous individuals having three different haplotypes (Lr-0.23, Lr-0.12, and Lr-0.21) were thus selected as donors; peripheral blood macrophages were then obtained and stimulated with Salmonella typhimurium (MOI 1:40). Although similarities were observed regarding peptide length distribution, elution patterns varied between individuals; in total, 1990 unique peptides were identified as follows: 372 for Pig 1 (Lr-0.23), 438 for Pig 2 (Lr.0.12) and 1180 for Pig 3 (Lr.0.21). Thirty-one S. typhimurium unique peptides were identified; most of the identified peptides belonged to outer membrane protein A and chaperonin GroEL. Notably, 87% of the identified bacterial peptides were predicted in silico to be elution ligands. These results encourage further in vivo studies to assess the immunogenicity of the identified peptides, as well as their usefulness as possible protective vaccine candidates.This research was funded by the Universidad de Ciencias Aplicadas y Ambientales (U.D.C.A) and the Fundación Instituto de Inmunología de Colombia (FIDIC), minute dated on 7 March 2023. The APC was funded by the Universidad Nacional de Colombia and the Universidad de Salamanca.Peer reviewedMultidisciplinary Digital Publishing InstituteUniversidad de Ciencias Aplicadas y Ambientales (Colombia)Fundación Instituto de Inmunología de ColombiaUniversidad Nacional de ColombiaUniversidad de SalamancaConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202520252024info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://hdl.handle.net/10261/381070reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)InglésThe underlying dataset has been published as supplementary material of the article in the publisher platform at DOI https://doi.org/10.3390/biology13100832https://doi.org/10.3390/biology13100832Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3810702026-05-22T06:33:51Z
dc.title.none.fl_str_mv Immunopeptidomics of Salmonella enterica Serovar Typhimurium-Infected Pig Macrophages Genotyped for Class II Molecules
title Immunopeptidomics of Salmonella enterica Serovar Typhimurium-Infected Pig Macrophages Genotyped for Class II Molecules
spellingShingle Immunopeptidomics of Salmonella enterica Serovar Typhimurium-Infected Pig Macrophages Genotyped for Class II Molecules
Celis-Giraldo, Carmen Teresa
Salmonella typhimurium
Immunopeptidomics
Peptide
Vaccine
Pig
title_short Immunopeptidomics of Salmonella enterica Serovar Typhimurium-Infected Pig Macrophages Genotyped for Class II Molecules
title_full Immunopeptidomics of Salmonella enterica Serovar Typhimurium-Infected Pig Macrophages Genotyped for Class II Molecules
title_fullStr Immunopeptidomics of Salmonella enterica Serovar Typhimurium-Infected Pig Macrophages Genotyped for Class II Molecules
title_full_unstemmed Immunopeptidomics of Salmonella enterica Serovar Typhimurium-Infected Pig Macrophages Genotyped for Class II Molecules
title_sort Immunopeptidomics of Salmonella enterica Serovar Typhimurium-Infected Pig Macrophages Genotyped for Class II Molecules
dc.creator.none.fl_str_mv Celis-Giraldo, Carmen Teresa
Suárez, Carlos F.
Agudelo, William
Ibarrola, Nieves
Dégano, Rosa M.
Díaz, Jaime
Manzano Román, Raúl
Patarroyo, M. A.
author Celis-Giraldo, Carmen Teresa
author_facet Celis-Giraldo, Carmen Teresa
Suárez, Carlos F.
Agudelo, William
Ibarrola, Nieves
Dégano, Rosa M.
Díaz, Jaime
Manzano Román, Raúl
Patarroyo, M. A.
author_role author
author2 Suárez, Carlos F.
Agudelo, William
Ibarrola, Nieves
Dégano, Rosa M.
Díaz, Jaime
Manzano Román, Raúl
Patarroyo, M. A.
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidad de Ciencias Aplicadas y Ambientales (Colombia)
Fundación Instituto de Inmunología de Colombia
Universidad Nacional de Colombia
Universidad de Salamanca
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Salmonella typhimurium
Immunopeptidomics
Peptide
Vaccine
Pig
topic Salmonella typhimurium
Immunopeptidomics
Peptide
Vaccine
Pig
description Salmonellosis is a zoonotic infection that has a major impact on human health; consuming contaminated pork products is the main source of such infection. Vaccination responses to classic vaccines have been unsatisfactory; that is why peptide subunit-based vaccines represent an excellent alternative. Immunopeptidomics was used in this study as a novel approach for identifying antigens coupled to major histocompatibility complex class II molecules. Three homozygous individuals having three different haplotypes (Lr-0.23, Lr-0.12, and Lr-0.21) were thus selected as donors; peripheral blood macrophages were then obtained and stimulated with Salmonella typhimurium (MOI 1:40). Although similarities were observed regarding peptide length distribution, elution patterns varied between individuals; in total, 1990 unique peptides were identified as follows: 372 for Pig 1 (Lr-0.23), 438 for Pig 2 (Lr.0.12) and 1180 for Pig 3 (Lr.0.21). Thirty-one S. typhimurium unique peptides were identified; most of the identified peptides belonged to outer membrane protein A and chaperonin GroEL. Notably, 87% of the identified bacterial peptides were predicted in silico to be elution ligands. These results encourage further in vivo studies to assess the immunogenicity of the identified peptides, as well as their usefulness as possible protective vaccine candidates.
publishDate 2024
dc.date.none.fl_str_mv 2024
2025
2025
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/381070
url http://hdl.handle.net/10261/381070
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv The underlying dataset has been published as supplementary material of the article in the publisher platform at DOI https://doi.org/10.3390/biology13100832
https://doi.org/10.3390/biology13100832
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute
publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,812455

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