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• W2021506996 abstract "Crosslinking of MHC class II (MHC-II) molecules by antibodies or by superantigens (SAg) induces a variety of functional responses in the antigen presenting cell. We were able to allocate K39 as the residue that is essential for binding of antibody L243 to the α chain of HLA-DR. K39 is also essential for binding of staphylococcal enterotoxin A (SEA). However, the functional responses of the two ligands differ considerably exemplified by the ability of L243 to induce apoptosis in monocytic cells and in B cells, whereas SEA is unable to activate the apoptosis pathway. Despite the differences in functional responses, both ligands induce cell aggregation in MonoMac-1 cells. The SEA molecule with its two different binding sites associates one MHC α chain with one β chain as opposed to two α chains that are brought into close proximity by the two identical antigen binding sites of L243. We therefore conclude that the spatial orientation of dimerized MHC-II and their associated proteins is an important factor for the nature of the transduced signal and consequently the outcome of functional responses." @default.
• W2021506996 created "2016-06-24" @default.
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• W2021506996 date "2006-12-01" @default.
• W2021506996 modified "2023-09-23" @default.
• W2021506996 title "The superantigen staphylococcal enterotoxin A (SEA) and monoclonal antibody L243 share a common epitope but differ in their ability to induce apoptosis via MHC-II" @default.
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• W2021506996 doi "https://doi.org/10.1016/j.imbio.2006.05.006" @default.
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