Por favor, use este identificador para citar o enlazar este Item:http://hdl.handle.net/20.500.12105/10783
Título
Multiple proteases process viral antigens for presentation by MHC class I molecules to CD8(+) T lymphocytes.
Autor(es)
Val, Margarita del ISCIII | Lopez, Daniel ISCIII
Fecha de publicación
2002-10
Cita
Mol Immunol . 2002 Oct;39(3-4):235-47
Idioma
Inglés
Tipo de documento
journal article
Resumen
Recognition by CD8(+) cytotoxic T lymphocytes of any intracellular viral protein requires its initial cytosolic proteolytic processing, the translocation of processed peptides to the endoplasmic reticulum via the transporters associated with antigen processing, and their binding to nascent major histocompatibility complex (MHC) class I molecules that then present the antigenic peptides at the infected cell surface. From initial assumptions that the multicatalytic and ubiquitous proteasome is the only protease capable of fully generating peptide ligands for MHC class I molecules, the last few years have seen the identification of a number of alternative proteases that contribute to endogenous antigen processing. Trimming by non-proteasomal proteases of precursor peptides produced by proteasomes is now a well-established fact. In addition, proteases that can process antigens in a fully proteasome-independent fashion have also been identified. The final level of presentation of many viral epitopes is probably the result of interplay between different proteolytic activities. This expands the number of tissues and physiological and pathological situations compatible with antigen presentation, as well as the universe of pathogen-derived sequences available for recognition by CD8(+) T lymphocytes.
MESH
Antigen Presentation | Animals | Antigen-Presenting Cells | Antigens, Viral | CD8-Positive T-Lymphocytes | Cysteine Endopeptidases | Endopeptidases | Histocompatibility Antigens Class I | Humans | Multienzyme Complexes | Proteasome Endopeptidase Complex | Receptors, Antigen, T-Cell
Versión en línea
DOI
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