Part:BBa_K1391005:Experience

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Applications of BBa_K1391005

This is a protein found natively in B cells. CD79 is a heterodimer of CD79A and CD79B that is part of signal transduction in the B-cell receptor. The IgM Heavy chain, IgM light chain, CD79A subunit, and CD79B subunit require processing in the ER and must all be expressed in order to membrane localize instead of being retained in the ER by quality checking mechanisms. Binding to the antigen (beta-amyloid) causes two BCR complexes to dimerize. This allowsLyn to phosphorylate the CD79 heterodimer which causes the recruitment of Syk. As a warning, recruited Syk can cause cross talk with native cell signaling pathways as can other proteins. Care must be taken to check protein interactions and point mutate Syk if needed. We attach a protease (TEV protease) to Syk and a transcriptional activator (Gal4-VP16) to CD79 using a cleavage site (TEV cleavage site). When The BCR is activated by our antigen, Syk-TEVp cleaves the cleavage sit and releases Gal4-VP16 which can activate a synthetic system.

B-cell receptors (BCRs) are naturally occurring, transmembrane protein complexes that consist of a membrane-bound antibody (IgM) and some associated proteins (CD79A and CD79B). Given that the variable region of the antibody can be specific for any of a large number of antigens, we designed a B-cell receptor to bind beta-amyloid plaques (a biomolecular hallmark of Alzheimer's disease). Once bound, activated receptors instigate intracellular signalling, which can then be manipulated to diagnose the disease.

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