Paula Wolf Bryant

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Before a class II molecule can be loaded with antigenic material and reach the surface to engage CD4+ T cells, its chaperone, the class II-associated invariant chain (Ii), is degraded in a stepwise fashion by proteases in endocytic compartments. We have dissected the role of cathepsin S (CatS) in the trafficking and maturation of class II molecules by(More)
Polysaccharides of pathogenic extracellular bacteria commonly have negatively charged groups or no charged groups at all. These molecules have been considered classic T cell-independent Ags that do not elicit cell-mediated immune responses in mice. However, bacterial polysaccharides with a zwitterionic charge motif (ZPSs), such as the capsular(More)
Determination of the crystal structure of class II: peptide complexes has shown that in addition to pocket interactions involving the side chains of the peptide, peptide binding to MHC class II molecules is characterized by a series of hydrogen bonds which are contributed by genetically conserved amino acid residues in the class II molecule to the main(More)
The loading of class II MHC molecules with antigenic peptides is largely confined to the endocytic vesicles of specialized antigen-presenting cells (APCs), such as B cells, macrophages and dendritic cells. At first glance, the pathway utilized by each of these professional APCs to generate class II-peptide complexes on their surface appears to be(More)
I-Ad molecules harboring single amino acid changes in the conserved 80-82 region of the beta-chain show altered trafficking in invariant chain (Ii)-negative cell lines. Since residues beta81 and beta82 form hydrogen bonds with the backbone of bound peptide, alterations in this region may result in distinct MHC class II conformers that are targeted(More)
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