Web of Science: 44 cites, Scopus: 45 cites, Google Scholar: cites,
Divergent paths for the selection of immunodominant epitopes from distinct antigenic sources
Kim, AeRyon (The Johns Hopkins University. School of Medicine)
Hartman, Isamu Z. (The Johns Hopkins University. School of Medicine)
Poore, Brad (Johns Hopkins University. School of Medicine)
Boronina, Tatiana (The Johns Hopkins University. School of Medicine)
Cole, Robert N. (The Johns Hopkins University. School of Medicine)
Song, Nianbin (The Johns Hopkins University. School of Medicine)
Ciudad, M. Teresa (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Caspi, Rachel R. (National Eye Institute)
Jaraquemada, Dolores (Universitat Autònoma de Barcelona. Departament de Biologia Cel·lular, de Fisiologia i d'Immunologia)
Sadegh-Nasseri, Scheherazade (Johns Hopkins University. School of Medicine)

Data: 2014
Resum: Immunodominant epitopes are few selected epitopes from complex antigens that initiate T cell responses. Here, to provide further insights into this process, we use a reductionist cell-free antigen processing system composed of defined components. We use the system to characterize steps in antigen processing of pathogen-derived proteins or autoantigens and we find distinct paths for peptide processing and selection. Autoantigen-derived immunodominant epitopes are resistant to digestion by cathepsins, whereas pathogen-derived epitopes are sensitive. Sensitivity to cathepsins enforces capture of pathogen-derived epitopes by Major Histocompatibility Complex class II (MHC class II) prior to processing, and resistance to HLA-DM-mediated-dissociation preserves the longevity of those epitopes. We show that immunodominance is established by higher relative abundance of the selected epitopes, which survive cathepsin digestion either by binding to MHC class II and resisting DM-mediated-dissociation, or being chemically resistant to cathepsins degradation. Non-dominant epitopes are sensitive to both DM and cathepsins and are destroyed.
Drets: Tots els drets reservats
Llengua: Anglès
Document: Article ; recerca ; Versió publicada
Matèria: Cathepsin ; Epitope capture ; HLA-DM ; Immunodominance ; Reductionist antigen processing
Publicat a: Nature communications, Vol. 5 (2014) , art. 5369, ISSN 2041-1723

DOI: 10.1038/ncomms6369
PMID: 25413013


30 p, 2.6 MB

El registre apareix a les col·leccions:
Documents de recerca > Documents dels grups de recerca de la UAB > Centres i grups de recerca (producció científica) > Ciències de la salut i biociències > Institut de Biotecnologia i de Biomedicina (IBB)
Articles > Articles de recerca
Articles > Articles publicats

 Registre creat el 2018-01-29, darrera modificació el 2021-08-08



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