Picture of Hao Wu

Hao Wu, Ph.D.

Asa and Patricia Springer Professor of Structural Biology, Professor of Biological Chemistry and Molecular Pharmacology, Boston Children's Hospital
Asa and Patricia Springer Professor of Structural Biology, Boston Children's Hospital

The Wu laboratory of structural and mechanistic immunology seeks to elucidate the mechanisms that govern the assembly and regulation of supramolecular complexes in innate immunity, with the ultimate goal of revealing targets for therapeutic intervention. Seeing is believing, and we hold structural insights as our guiding principle to understand complex biological questions. Our current research focuses on inflammasomes, which are a family of cellular machines for activating inflammatory caspases. Activated caspases process the IL-1 family cytokines and the pore forming protein gasdermin D (GSDMD), and GSDMD pores release the mature cytokines and cause pyroptotic cell death. In addition, we continue to study the tumor necrosis factor (TNF) receptor and Toll-like receptor (TLR) pathways.

There are thus three pillars to my research program: 1) cryo-EM and other biophysical methods to understand molecular complexes, 2) structure-directed discovery of therapeutics in immune diseases and cancer, and 3) cellular imaging and other tools to study the assembly of supramolecular complexes in cells. Our studies have identified and strengthened our knowledge of supramolecular assemblies in innate immunity. This knowledge is also contributing to therapeutic development for aging- and life-style-related diseases, including cardiovascular, neurodegenerative, and metabolic diseases.

Address: 

Center for Life Sciences Bldg, room 3099

3 Blackfan Circle

Boston, MA 02115

Publications View
DNA melting initiates the RAG catalytic pathway.
Authors: Authors: Ru H, Mi W, Zhang P, Alt FW, Schatz DG, Liao M, Wu H.
Nat Struct Mol Biol
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The Structure of the Necrosome RIPK1-RIPK3 Core, a Human Hetero-Amyloid Signaling Complex.
Authors: Authors: Mompeán M, Li W, Li J, Laage S, Siemer AB, Bozkurt G, Wu H, McDermott AE.
Cell
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Cryo-EM structure of the gasdermin A3 membrane pore.
Authors: Authors: Ruan J, Xia S, Liu X, Lieberman J, Wu H.
Nature
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AID Recognizes Structured DNA for Class Switch Recombination.
Authors: Authors: Qiao Q, Wang L, Meng FL, Hwang JK, Alt FW, Wu H.
Mol Cell
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Inflammasome-activated gasdermin D causes pyroptosis by forming membrane pores.
Authors: Authors: Liu X, Zhang Z, Ruan J, Pan Y, Magupalli VG, Wu H, Lieberman J.
Nature
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The Structure and Dynamics of Higher-Order Assemblies: Amyloids, Signalosomes, and Granules.
Authors: Authors: Wu H, Fuxreiter M.
Cell
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Molecular Mechanism of V(D)J Recombination from Synaptic RAG1-RAG2 Complex Structures.
Authors: Authors: Ru H, Chambers MG, Fu TM, Tong AB, Liao M, Wu H.
Cell
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Cryo-EM structure of the activated NAIP2/NLRC4 Inflammasome reveals nucleated polymerization
Authors: Authors: Zhang L, Shuobing C, Jianbin R, Wu J, Tong AB, Yin Q, Li Y, David L, Lu A, Wang WL, Marks C, Ouyang Q, Zhang X, Mao Y, Wu H
Science
Unified polymerization mechanism for the assembly of ASC-dependent inflammasomes.
Authors: Authors: Lu A, Magupalli VG, Ruan J, Yin Q, Atianand MK, Vos MR, Schröder GF, Fitzgerald KA, Wu H, Egelman EH.
Cell
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Higher-order assemblies in a new paradigm of signal transduction.
Authors: Authors: Wu H.
Cell
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