Welcome to

The Wu Lab

The Wu laboratory of mechanistic immunology focuses on elucidating cellular and structural regulation in innate immune pathways, in particular the inflammasome pathway.


Congratulations to Venkat and Roberto for their recent Science paper, "HDAC6 mediates an aggresome-like mechanism for NLRP3 and pyrin inflammasome activation"

September 2020 | PDF

"Inflammasomes are supramolecular complexes that play key roles in immune surveillance. This is accomplished by the activation of inflammatory caspases, which leads to the proteolytic maturation of interleukin 1β (IL-1β) and pyroptosis. Here, we show that nucleotide-binding domain, leucine-rich repeat, and pyrin domain-containg protein 3 (NLRP3)- and pyrin-mediated inflammasome assembly, caspase activation, and IL-1β conversion occur at the microtuble-organizing center (MTOC)." Continue Reading 

Congratulations to Jacob and Shiyu for their recent Nature Immunology paper, "FDA-approved disulfiram inhibits pyroptosis by blocking gasdermin D pore formation"


"Inflammation is the alarm system by which cells first respond to potential danger, but in excess, inflammation can be fatal. In COVID-19, for example, overactive inflammation has led to severe complications and even death for many hospitalized patients. Research in mice led by Harvard Medical School and Boston Children’s Hospital now reveals that the FDA-approved drug disulfiram, commonly used for treating alcoholism, blocks a key gatekeeper protein involved in inflammation.Continue reading

May 2020 | PDF | HMS News & Research Article

Congratulations to Humayun, Li, and Weili for their recent Nature paper, "Structural mechanism for NEK7-licensed activation of NLRP3 inflammasome"

June 2019 | PDF | Nature News & Views Feature Article

"The NLRP3 inflammasome can be activated by stimuli that include nigericin, uric acid crystals, amyloid-β fibrils and extracellular ATP. The mitotic kinase NEK7 licenses the assembly and activation of the NLRP3 inflammasome in interphase. Here we report a cryo-electron microscopy structure of inactive human NLRP3 in complex with NEK7, at a resolution of 3.8 Å. The earring-shaped NLRP3 consists of curved leucine-rich-repeat and globular NACHT domains..." Continue reading

Swell Snapshots | Harvard Medical School News & Research

"After decades of attempts by the scientific community, researchers at Harvard Medical School and Peking University have provided the first clear look at a protein implicated in a vast array of inflammatory conditions. The finding, published June 12 in Nature, lifts a blindfold that has hampered scientists' ability to intervene when the immune system overreacts to perceived threats..." Continue Reading 


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Boston Children's Hospital

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Boston, MA 02115

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