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• W2134261692 startingPage "63" @default.
• W2134261692 abstract "<h2>Abstract</h2> Using expression cloning, we have identified an <i>H2-M3</i>-restricted epitope of the intracellular bacterial pathogen Listeria monocytogenes. Picomolar concentrations of an amino-terminal N-formylated hexapeptide, fMIGWII, targeted cells for lysis by CD8⁺ cytotoxic T cells, while the nonformylated peptide was approximately 100-fold less active. The sequence of the 185 aa protein source of this epitope predicts a transmembrane protein that retains its N terminus and assumes an N_out–C_in topology. This membrane orientation offers an explanation for the protection of the epitope from deformylases present in the bacterial cell and suggests an explanation for the ability of phagocytes to present <i>H2-M3</i>-restricted bacterial epitopes via a vacuolar TAP-independent mechanism." @default.
• W2134261692 created "2016-06-24" @default.
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• W2134261692 date "1996-07-01" @default.
• W2134261692 modified "2023-10-11" @default.
• W2134261692 title "Identification of an H2-M3-Restricted Listeria Epitope: Implications for Antigen Presentation by M3" @default.
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• W2134261692 doi "https://doi.org/10.1016/s1074-7613(00)80310-6" @default.
• W2134261692 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2778046" @default.
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• W2134261692 hasPublicationYear "1996" @default.
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