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• W2949276665 abstract "B cells encounter antigen over a wide range. The strength of B cell signaling in response to antigen increases with affinity, a process known as affinity discrimination. In this work, we use a computational simulation of B cell surface dynamics and signaling to show that discrimination can arise from the formation of BCR oligomers. It is known that BCRs form oligomers upon encountering antigen, and that the size and rate of formation of these oligomers increase with affinity. In our simulation, we have introduced a requirement that only BCR-antigen complexes that are part of an oligomer can engage cytoplasmic signaling molecules such as Src-family kinases. Our simulation shows that as increases, not only does the number of collected antigen increases, but so does signaling activity. Our results are also consistent with the existence of an experimentally-observed threshold of activation (no signaling activity below this value) and discrimination ceiling (no discrimination above this value). Comparison with experiments shows that the time scale of dimer formation predicted by our model (less than 10 s) is well within the time scale of experimentally observed association of BCR with Src-family kinases (10-20 s)." @default.
• W2949276665 created "2019-06-27" @default.
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• W2949276665 date "2012-02-21" @default.
• W2949276665 modified "2023-09-27" @default.
• W2949276665 title "Formation of BCR Oligomers Provides a Mechanism for B cell Affinity Discrimination" @default.
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• W2949276665 hasPublicationYear "2012" @default.
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