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• W2094022017 abstract "Summary Plasma membrane rafts are sphingolipid‐ and cholesterol‐rich patches that function as membrane trafficking and surface signalling regions. Ganglioside G M1 is an integral component of these microdomains, and Escherichia coli enterotoxin B subunit (EtxB) is a pentamer that binds with high affinity to G M1 resulting in G M1 cross‐linking. We previously demonstrated that antigen coupled directly to EtxB resulted in enhanced presentation relative to antigen taken up by fluid‐phase endocytosis. Here we demonstrate a new role for G M1 in antigen presentation by examining the effects of cross‐linking G M1 on the kinetics of presentation and processing of antigen by the B‐cell receptor (BCR), fluid‐phase endocytosis and G M1 ‐targeted antigen. EtxB bound to B cells does not augment the subsequent kinetics or magnitude of presentation of either BCR‐internalized antigen or soluble antigen. Moreover, presentation of G M1 ‐bound antigen is significantly slower than antigen presentation following BCR‐mediated uptake. In contrast to the rapid internalization of BCR‐bound antigen (which has a half life of 60 min), the majority of EtxB‐bound antigen forms a plasma membrane depot detectable for many hours after initial incubation (and with a half life of 12 hr). We conclude that cross‐linking of G M1 by EtxB minimally affects the processing and presentation of antigens internalized via other pathways. Nevertheless, binding of antigens to G M1 results in delayed presentation that has important implications for in vivo immunization using G M1 ‐targeted adjuvants." @default.
• W2094022017 created "2016-06-24" @default.
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• W2094022017 creator A5059163386 @default.
• W2094022017 creator A5061032580 @default.
• W2094022017 date "2002-04-24" @default.
• W2094022017 modified "2023-09-29" @default.
• W2094022017 title "Antigen binding to GM1 ganglioside results in delayed presentation: minimal effects of GM1 on presentation of antigens internalized via other pathways" @default.
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• W2094022017 doi "https://doi.org/10.1046/j.1365-2567.2002.01397.x" @default.
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