Academic Profile : Faculty

Assoc Prof Wu Bin.jpg picture
Assoc Prof Wu Bin
Associate Professor, School of Biological Sciences

School of Biological Sciences, Nanyang Technological University, Singapore
Ph.D. in Biochemistry, Biophysics and Structural Biology, 2006.07-2010.02
B.Sc. in Biological Sciences, 2002.07-2006.06

Research Experience

Charles A. King Research Fellow, Harvard Medical School, 2010-present
Advisor: Sun Hur
Dissected the molecular mechanisms for viral RNA recognition and signaling by RIG-I/MDA5 and MAVS, an important innate immune signaling pathway related to multiple diseases. Investigated viral dsRNA recognition process of MDA5 by using techniques including biochemistry, molecular biology, X-ray crystallography and electron microscopy (Wu et al, Cell, 2013). This work is exclusively highlighted in Nature Review Immunology 2013. Established an in vitro reconstituted assay system to study MAVS signaling, which was applied to study related innate immune receptors and lead to the identification of RNA dependent filament formation as an important signaling mechanism in innate immunity (Peisley & Wu et al, Mol Cell, 2013) & (Peisley, Wu, et al, Nature, 2014). In addition, I also solved the MAVS filament structure (Wu et al, Mol Cell, 2014).

Graduate Student, Nanyang Technological University, 2006-2010
Advisor: Curt A. Davey
Using a combination of biochemical and biophysical tools, I characterized the molecular basis of therapeutic effects of Pt based anti-cancer drugs. Demonstrated how these drugs inhibited the dynamics of the basic functional units of our genome, the nucleosomes (Wu et al, Nature Chemical Biology, 2008). This work is also highlighted in Nature 2008. Additional work on biochemical and structural studies of nucleosomes with a variety of DNA sequences or modified DNA directly demonstrated the evidence of DNA sequence dependent nucleosome.
Auto-immune diseases are often caused by mis-regulated innate immune responses. The recent discoveries of a collection of innate immune receptors and their downstream adaptors provided us with the unprecedented opportunities to investigate and tackle the related diseases. However, at the moment, the effort of developing related therapies is largely prohibited by a lack of knowledge of molecular information of the key components of the signaling pathways.

Based on my previous success and experience in characterizing MDA5 and RIG-I, two cellular viral RNA sensors in innate immunity, I propose to investigate their downstream adaptor protein, MAVS, and other related innate immune signaling pathways. I plan to employ a combination of biophysical, biochemical and cellular methodologies to achieve my research goals.

I encourage undergraduate and graduate students sending in enquiries about opportunities performing cutting-edge research in molecular immunology. There are also Project Officer positions available.

please email for further information.
  • Determining the molecular and structural basis for inflammasome activation in human (OFIRG19may-0073)
  • Determining the molecular basis of Noddosome activation in human
  • Human NLRP1 as a nuclear dsRNA sensor
  • Identification and characterization of novel cellular factors that license the human NLRP1 inflammasome to sense dsRNA
  • Structural basis of filamin A mediated regulation of b2 integrins
  • The Role of Setd3 in Regulation of B Cell Activation and Differentiation
  • Transfection-free in situ engineering of Receptors and Protein-based signaling molecules
US 2019/0218586 A1: Methods For Enzymatic Peptide Ligation (2023)
Abstract: The present invention relates to a method of ligating a first peptide via its C-terminus to the N-terminus of a second peptide, wherein the reaction is catalyzed by an asparagine/aspartate (Asx) peptide ligase OaAEPI Cys247Ala having the amino acid sequence of SEQ ID NO: 1. Further encompassed are a method of preparing a dimer, oligomer, or multimer of one or more peptides of interest and a method of modifying or tagging the surface of a target cell by one or more peptides of interest. Also encompassed in the invention are the ligated peptides and/or tagged target cells obtainable according to any of the methods, the peptide ligase OaAEPI Cys247Ala having the amino acid sequence of SEQ ID NO: 1, as well as kits comprising said peptide ligase.