A major component of adaptive immunity is B cells, which produce antibodies. Fc Receptor-like 1 (FCRL1) is a receptor protein on B cells that interacts with the protein SHIP-1, but the details of this interaction are not well understood. SHIP-1 has 3 important domains: SH2, phosphatase, and proline-rich region. We seek to determine more about the relationship between SHIP-1 and FCRL1, specifically which domain of SHIP-1 is participating in the interaction. To study the individual domains of SHIP-1 and determine which interacts with FCRL-1, we will express these three domains individually (fused to green fluorescent protein, or GFP) in cells using a lentiviral expression vector. Cells that successfully take up and express the vector will fluoresce due to GFP, and we will isolate these cells using fluorescence-activated cell sorting. Once the cells are expressing the individual domains of SHIP-1 fused to GFP, a co-immunoprecipitation will be performed to determine which domain of SHIP-1, if any, interacts with FCRL1. This research project helps us gain a better understanding of B cell biology, including the role of FCRL1 in both activation and inhibition of a B cell response. The results will allow us to work out some of the finer details of the immune system and have implications in autoimmune disease prevention and treatment, as well as the immune response to infection.
Author: Elizabeth Zenni, Microbiology
Advisor: Timothy Wilson, Microbiology
Graduate Advisor: Malory Wilson
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