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Shern, T.

Publications and source records attributed to Shern, T..

2 recordsLinked to original sources

Cytokinesis Arrest-induced Binucleation of Macrophages ProducesHighly Efficient Efferocytes

Efferocytosis, the phagocytic clearance of dying cells and debris, supports tissue homeostasis, immune tolerance, and inflammation resolution, whereas its failure contributes to autoimmunity, atherosclerosis, aging, and impaired tissue repair. Although many molecular regulators of efferocytosis have been defined, less is known about whether macrophages can be reprogrammed into a distinct cellular state with intrinsically enhanced efferocytosis capacity. Guided by a CRISPR screen, we found that Pdcd6ip loss induces cytokinesis arrest and binucleation, creating macrophages with superior efferocytic function. Binucleated Pdcd6ip-/- bone marrow-derived macrophages demonstrate a coordinately enhanced multi-corpse capture and processing, and resolution response, and acquired a distinct transcriptomic signature. In vivo, Pdcd6ip deletion enhanced splenic macrophage efferocytosis, reduced autoimmune responses after repeated apoptotic cell challenge, and promoted plaque stability without metabolic or hematologic changes. PDCD6IP perturbation similarly increased binucleation and engulfment in human macrophage-like cells. Thus, incomplete cytokinesis represents an unrecognized route to macrophage specialization with enhanced efferocytosis capacity.

cell biology↗

TurboID-mediated surface protein biotinylation to inhibit the growth of Staphylococcus aureus

Staphylococcus aureus (S. aureus) infection is major cause of nosocomial infections. Antibiotic treatment for S. aureus remains the primary solution for managing S. aureus infections, which, however, increases the risk of antibiotic resistance. To broaden the resolutions on S. aureus infection, here we report TurboID-mediated protein proximity technologies to inhibit the growth of S. aureus. To achieve this goal, we utilized synthetic biology techniques to create a fusion protein named N-AgrD-TurboID (Agr-ID). The N-AgrD domain includes auto-inducer peptide (AIP) which combined to the surface AgrC protein on S. aureus. As such, TurboID then catalyzed the production of biotinoyl-5-AMP anhydride, triggering the biotinylation of surface proteins on S. aureus 25923 which were visualized by using fluorescence microscopy after incubating with Alexa Fluor 647-conjugated streptavidin. The biotinylation of surface protein on S. aureus 25923, S. aureus 43300, and S. aureus 6538 (MRSA) also resulted in growth inhibition and impaired colonization. Moreover, the biotinylation on surface protein further inhibited virulence protein production in S. aureus 25923, as indicated by reduced apoptosis of HEK 293T cells after treatment with S. aureus 25923 lysates. Overall, our work reveals that the biotinylation of surface proteins can inhibit the growth and toxicity of S. aureus 25923, S. aureus 43300, and S. aureus 6538 (MRSA), indicating therapeutic potential in clinical treatment.

microbiology↗