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个人简介
My laboratory focuses on two major aspects of nucleic acid-induced innate immune activation. First, we seek to understand the mechanisms by which post-transcriptional gene regulation is orchestrated during periods of innate immune activation, particularly focusing on how RNA-binding proteins (RBPs) and their cognate RNA substrates are regulated during viral infection. These substrates can originate from the host or pathogen, a molecular challenge faced by cellular RBPs during active viral infection. My laboratory has a core set of expertise towards the identification of RNA-protein interactions at a transcriptome-wide scale. I co-developed PAR-CLIP, a photochemical biology and high-throughput sequencing approach utilizing photoreactive ribonucleoside analogs to covalently attach RNA-binding proteins to their cognate targets in living cells. We expanded on this technology to investigate host-pathogen interactions between cellular proteins and viral RNA using a new approach my laboratory developed, called VIR-CLASP (Kim and Arcos et al. 2020b). Using VIR-CLASP, we identified hundreds of proteins that directly interacted with the Chikungunya (CHIKV) and Influenza Type A ssRNA genomes, within minutes of infection (Kim and Arcos et al. 2020a), and characterized three novel RNA-binding protein families that played essential pro- or anti-viral roles. We demonstrated that VIR-CLASP is extensible to virtually all RNA virus families, including Coronaviridae. We were also able to use VIR-CLASP to precisely mark the period of flaviviral entry and demonstrated how ER-membrane complex members contributed to entry and exit of viral particles (Barrows et al., 2019). The second major aspect that I am in interested in understanding is how pathogenic DNA stimulates innate immunity. My lab has made significant progress on understanding the cGAS pattern recognition receptor and enzyme, which I had originally discovered to produce a novel asymmetric phosphodiester linkage. My lab identified the first potent and selective small molecule antagonist that inhibits mouse (Vincent et al., 2017) and human (Wiser et al., 2020) cGAS enzymatic activity. In collaboration, we have also reported on the encapsulation of cGAMP as a means of enhancing delivery of this second messenger to cells for their potent immune activation (Shae et al., 2019). The analytical, biochemical, and cell biological tools that I established to characterize cGAS and its downstream partner STING places me in the unique position of investigating post-transcriptional gene regulatory mechanisms as a function of a nucleic acid-induced innate immune pathway.
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Cell Reportsno. 8 (2021): 109178-109178
SCIENTIFIC REPORTSno. 1 (2018): 588-588
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#Papers: 50
#Citation: 8104
H-Index: 26
G-Index: 40
Sociability: 5
Diversity: 3
Activity: 31
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