About

Jueqi Chen is a researcher at the University of Chicago, leading a lab focused on host-pathogen interactions. Their research investigates how infections by viruses and bacteria remodel host cell organelles to either promote disease progression or activate the host's innate immune responses. The lab aims to explore innovative therapeutic strategies against infectious diseases, inflammatory disorders, autoimmune diseases, and cancer. Key contributions include uncovering mechanisms of organelle remodeling in innate immunity, such as how bacterial toxins are internalized to reorganize the trans-Golgi network and activate the NLRP3 inflammasome, and how cholesterol-dependent cytolysins form structures on the TGN to stimulate inflammatory cytokine production. Additionally, the lab has identified a novel membrane structure called 3a dense bodies (3DBs) during SARS-CoV-2 infection, which are involved in viral protein processing and entry efficiency. The research employs diverse approaches, including biochemical assays, high-resolution fluorescence imaging, CRISPR technology, and mouse models, with part of the lab stationed at the Howard Taylor Ricketts Laboratory, a BSL3 facility dedicated to studying SARS-CoV-2 pathogenesis.

Research topics

• Biology
• Cell biology
• Biochemistry
• Immunology
• Chemistry
• Virology

Selected publications

• Clinicoradiomic analysis for predicting short-term treatment efficacy after one session of ultrasound-guided extracorporeal wave lithotripsy in patients with a single ureteral stone

  Urolithiasis · 2026-04-21

  articleSenior author
  PublisherDOI

• Sensing the spectrum: diverse stimuli for the NLRP3 inflammasome

  Communications Biology · 2026-05-20

  articleOpen accessSenior author

  The NLRP3 inflammasome is a central inflammatory signaling pathway in host defense, cancer, metabolic disorders, and neurodegenerative diseases. Unlike other pattern-recognition receptors, NLRP3 senses perturbations in organelle integrity and ion homeostasis, enabling its activation by a remarkably broad spectrum of pathogen-derived and cellular stress signals. In this review, we summarize recent advances that have expanded our understanding of the diverse classes of NLRP3 stimuli and highlight breakthroughs in elucidating the molecular mechanisms underlying both infection-driven and sterile inflammation. Finally, we discuss unresolved questions surrounding the physiological relevance of NLRP3 stimuli and the nature of uncharacterized stimuli in sterile inflammatory diseases, emphasizing how resolving these gaps may inform targeted therapeutic development.

  PublisherDOI

• SARS-CoV-2 ORF3a drives dynamic dense body formation for optimal viral infectivity

  Nature Communications · 2025-05-12 · 11 citations

  articleOpen accessSenior author

  SARS-CoV-2 hijacks multiple organelles for virion assembly, of which the mechanisms have not been fully understood. Here, we identified a SARS-CoV-2-driven membrane structure named the 3a dense body (3DB). 3DBs are unusual electron-dense and dynamic structures driven by the accessory protein ORF3a via remodeling a specific subset of the trans-Golgi network (TGN) and early endosomal membrane. 3DB formation is conserved in related bat and pangolin coronaviruses but was lost during the evolution to SARS-CoV. During SARS-CoV-2 infection, 3DB recruits the viral structural proteins spike (S) and membrane (M) and undergoes dynamic fusion/fission to maintain the optimal unprocessed-to-processed ratio of S on assembled virions. Disruption of 3DB formation resulted in virions assembled with an abnormal S processing rate, leading to a dramatic reduction in viral entry efficiency. Our study uncovers the crucial role of 3DB in maintaining maximal SARS-CoV-2 infectivity and highlights its potential as a target for COVID-19 prophylactics and therapeutics. Hartmann et al. discovered that SARS-CoV-2 constructs a group of dynamic membrane structures named the 3DB. 3DB regulates the processing of the viral spike protein to assemble a highly infectious virus, highlighting the potential of 3DB as a novel COVID-19 therapeutic target.

  PublisherOA PDFDOI

• Type A cholesterol-dependent cytolysins translocate to the trans-Golgi network for NLRP3 inflammasome activation

  Nature Immunology · 2025-09-05 · 4 citations

  articleOpen accessSenior author
  PublisherOA PDFDOI

• SARS-CoV-2 ORF3a drives dynamic dense body formation for optimal viral infectivity

  Research Square (Research Square) · 2024

  Senior authorCorresponding
  • Cell biology
  • Biology
  • Virology

  -Golgi network (TGN) and early endosomal membranes. 3DB formation is conserved in related bat and pangolin coronaviruses yet lost during the evolution to SARS-CoV. 3DBs recruit the viral structural proteins spike (S) and membrane (M) and undergo dynamic fusion/fission to facilitate efficient virion assembly. A recombinant SARS-CoV-2 virus with an ORF3a mutant specifically defective in 3DB formation showed dramatically reduced infectivity for both extracellular and cell-associated virions. Our study uncovers the crucial role of 3DB in optimal SARS-CoV-2 infectivity and highlights its potential as a target for COVID-19 prophylactics and therapeutics.

  PublisherOA PDFDOI

• Comparison of ureteral stone measurements for predicting the efficacy of a single session of extracorporeal shockwave lithotripsy: one-, two-, and three-dimensional computed tomography measurements

  Urolithiasis · 2024-03-05 · 2 citations

  article
  PublisherDOI

• NLRP9 in innate immunity and inflammation

  Immunology · 2020 · 29 citations

  Senior authorCorresponding
  • Biology
  • Immunology
  • Cell biology

  The nucleotide-binding domain leucine-rich repeat containing receptors (NLRs) are a family of evolutionarily conserved proteins. Several members of NLRs, notably NLRP1, NLRP3 and NLRC4, are able to form cytosolic oligomeric signalling platforms termed inflammasomes to mediate immune response towards pathogens, damage and stress. However, the functions of many NLRs still remain elusive. In the past few years, a couple of less-characterized NLR members are emerging as important signalling molecules with fundamental functions in host defence and inflammation. Among them, NLRP9 is an NLR originally proposed to be expressed and function solely in the reproductive system. Recent evidence has suggested that NLRP9 is also capable of initiating inflammasome formation in the intestine to restrict replication and damage brought by rotavirus infection. Here, we highlight the latest progress in characterization of the role of NLRP9 in infectious and inflammatory diseases, as well as the newest crystallographic and biochemical studies on NLRP9. Finally, we discuss some important questions remained to be answered regarding the molecular and cellular mechanisms governing NLRP9's function in innate immunity and inflammation.

  PublisherOA PDFDOI

• Direct, Noncatalytic Mechanism of IKK Inhibition by A20

  UNC Libraries · 2020-11-06

  articleOpen access

  A20 is a potent anti-inflammatory protein that inhibits NF-κB, and A20 dysfunction is associated with autoimmunity and B-cell lymphoma. A20 harbors a deubiquitination enzyme domain and can employ multiple mechanisms to antagonize ubiquitination upstream of NEMO, a regulatory subunit of the IκB kinase complex (IKK). However, direct evidence of IKK inhibition by A20 is lacking, and the inhibitory mechanism remains poorly understood. Here we show that A20 can directly impair IKK activation without deubiquitination or impairment of ubiquitination enzymes. We find that polyubiquitin binding by A20, which is largely dependent on A20’s seventh zinc finger motif (ZnF7), induces specific binding to NEMO. Remarkably, this ubiquitin-induced recruitment of A20 to NEMO is sufficient to block IKK phosphorylation by its upstream kinase TAK1. Our results suggest a non-catalytic mechanism of IKK inhibition by A20 and a means by which polyubiquitin chains can specify a signaling outcome.

  PublisherDOI

• PtdIns4P on dispersed <i>trans</i>-Golgi network mediates NLRP3 inflammasome activation

  The Journal of Immunology · 2019-05-01

  article1st authorCorresponding

  Abstract The NLRP3 inflammasome, which has been linked to human inflammatory diseases, is activated by diverse stimuli. How these stimuli activate NLRP3 is unknown. Here we show that different NLRP3 stimuli lead to disassembly of the trans-Golgi network (TGN). NLRP3 is recruited to the dispersed TGN (dTGN) through ionic bonding between its conserved polybasic region and negatively charged phosphatidylinositol-4-phosphate (PtdIns4P) on the dTGN. The dTGN then serves as a scaffold for NLRP3 aggregation into multiple puncta, leading to polymerization of the adaptor protein ASC, thereby activating the downstream signalling cascade. Disruption of the interaction between NLRP3 and PtdIns4P on the dTGN blocked NLRP3 aggregation and downstream signalling. These results indicate that recruitment of NLRP3 to dTGN is an early and common cellular event that leads to NLRP3 aggregation and activation in response to diverse stimuli.

  PublisherDOI

• PtdIns4P on dispersed trans-Golgi network mediates NLRP3 inflammasome activation

  Nature · 2018-11-27 · 671 citations

  articleOpen access1st authorCorresponding
  PublisherOA PDFDOI

Frequent coauthors

• Zhijian J. Chen

  Howard Hughes Medical Institute

  14 shared

• Luis Martínez‐Sobrido

  9 shared

• Lijun Sun

  4 shared

• Chengjin Ye

  Texas Biomedical Research Institute

  3 shared

• Stella Hartmann

  University of Chicago

  3 shared

• Lisa Radochonski

  University of Chicago

  3 shared

• Xiang Chen

  Yangzhou University

  2 shared

• Xin Cai

  2 shared

Education

• PhD

  University of Texas Southwestern Medical Center at Dallas

  2014

• Bachelor of Science

  Zhejiang University

  2009