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- W4313355839 abstract "Abstract The exact mechanisms of antigen processing within an antigen presenting cell (APC) are not well defined. The canonical pathway describes degradation of the antigenic proteins, competition between peptides for binding to MHC II, followed by presentation to T cells. Alternately, an entire protein might bind to MHC II first and be trimmed through the action of enzymes. Here we determined the binding affinity of HA to DR1, a human MHC II allele, in the presence and absence of the peptide-editing molecule DM and whether multiple DR1 can bind to a single HA. Binding affinities were determined by competitive binding assays with or without DM. Both native and denatured HA bind to DR1 with comparable affinities in the hundreds of nanomolar range. DM appears to decrease binding strength of HA irrespective of its state. Multiple binding events on individual HA were shown over time on blue native-PAGE gels. Bands of increasing molecular weight appear over a 24-hour time course in the blue native gels while amounts of HA and DR1 decrease over time. Taken together, these results support the hypothesis of an alternate pathway of antigen processing whereby the protein binds first to potentially multiple MHC II molecules and is then trimmed by enzymatic activity. Such MHC-mediated shielding mechanism may increase presentation of peptides by APCs that would be otherwise lost to cleavage." @default.
- W4313355839 created "2023-01-06" @default.
- W4313355839 creator A5036259271 @default.
- W4313355839 creator A5049078317 @default.
- W4313355839 date "2017-05-01" @default.
- W4313355839 modified "2023-09-27" @default.
- W4313355839 title "MHC II binds to multiple sites on H1N1 hemagglutinin protein" @default.
- W4313355839 doi "https://doi.org/10.4049/jimmunol.198.supp.209.4" @default.
- W4313355839 hasPublicationYear "2017" @default.
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