ArticleProtein expression and purification2025
Refolding of the recombinant IgV domain of CD47 from E. coli for NMR studies.
Article in Protein expression and purification, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
CD47 is a widely expressed integrin-associated transmembrane protein that regulates many macrophage functions, including phagocytosis. Since many cancer cells overexpress CD47 to evade the immune system, targeting CD47 has been proposed as a strategy to enhance macrophage-mediated destruction of cancer cells. Consequently, developing antagonists that block the CD47-SIRPα interaction has drawn attention. However, the exclusive use of eukaryotic cell culture to produce CD47-IgV precludes isotope enrichment of the domain. This prevents the use of solution NMR as a tool for identifying CD47 inhibitors. Here, we describe a two-step refolding protocol for the CD47-IgV domain from inclusion bodies produced in E. coli. The yield of CD47-IgV is ∼30 mg/L of culture. The refolded domain interacts with the anti-CD47 antibody B6H12 with an affinity similar to glycosylated CD47-IgV produced in mammalian cells and binds the IgV domain of SIRPα. The method allowed us to produce
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