MHC Class I Peptide Binding and Tapasin
نویسندگان
چکیده
منابع مشابه
Tapasin is a facilitator, not an editor, of class I MHC peptide binding.
Tapasin has been proposed to function as a peptide editor to displace lower affinity peptides and/or to favor the binding of high affinity peptides. Consistent with this, cell surface HLA-B8 molecules in tapasin-deficient cells were less stable and the peptide repertoire was substantially altered. However, the binding affinities of peptides expressed in the absence of tapasin were unexpectedly ...
متن کاملTapasin enhances MHC class I peptide presentation according to peptide half-life.
Understanding how peptides are selected for presentation by MHC class I is crucial to vaccination strategies based on cytotoxic T lymphocyte priming. We have studied this selection of the MHC class I peptide repertoire in terms of the presentation of a series of individual peptides with a wide range of binding to MHC class I. This series was expressed as minigenes, and the presentation of each ...
متن کاملDirect peptide-regulatable interactions between MHC class I molecules and tapasin.
Tapasin (Tpn) has been implicated in multiple steps of the MHC class I assembly pathway, but the mechanisms of function remain incompletely understood. Using purified proteins, we could demonstrate direct binding of Tpn to peptide-deficient forms of MHC class I molecules at physiological temperatures. Tpn also bound to M10.5, a pheromone receptor-associated MHC molecule that has an open and emp...
متن کاملTAP- and tapasin-dependent HLA-E surface expression correlates with the binding of an MHC class I leader peptide
BACKGROUND The human major histocompatibility complex (MHC) class lb molecule HLA-E is transcribed in most tissues but little is known about its localisation within the cell. We have recently shown that HLA-E binds signal-sequence-derived peptides from human MHC class I molecules in vitro. RESULTS Using a newly characterised antibody recognising HLA-E, we show that HLA-E is expressed at the c...
متن کاملThe binding of TAPBPR and Tapasin to MHC class I is mutually exclusive.
The loading of peptide Ags onto MHC class I molecules is a highly controlled process in which the MHC class I-dedicated chaperone tapasin is a key player. We recently identified a tapasin-related molecule, TAPBPR, as an additional component in the MHC class I Ag-presentation pathway. In this study, we show that the amino acid residues important for tapasin to interact with MHC class I are highl...
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ژورنال
عنوان ژورنال: The Journal of Immunology
سال: 2003
ISSN: 0022-1767,1550-6606
DOI: 10.4049/jimmunol.171.1.3