Tao Ni

2008-2012 Bachelor of Science, Nankai University

2012-2016 PhD in Structural Biology, University of Oxford

2016-2022 Postdoc, University of Oxford

2022 – present Assistant Professor, University of Hong Kong

My lab specializes the state-of-the-art structural biology methods and address key biological questions. Biologically, we primarily focus on the interface between host and pathogens (virus and parasites) to decipher their relationship in the molecular level, utilizing cutting-edge structural biology approaches. Our current objective is to understand the fundamental principles of positive-stranded RNA virus replication in host cells, including coronavirus (such as SARS-CoV, MERS-CoV and SARS-CoV-2) and Flavivirus (Dengue virus, Hepatitis C virus and ZIKA), all of which are important pathological viruses threatening human’s life and health. Based on these mechanistic discoveries, we aim to developing new generation of antivirals and vaccines to combat infections and related diseases. Currently, we are:

1) Deciphering the structure and function of the molecular complexes relating to Coronavirus replication organelle using an integrative biochemical, biophysical and structural methods (including in vitro biochemical reconstitution, X-ray crystallography, cryo-EM and cryo-ET subtomogram averaging, etc);

2) Investigating the principles of virus assembly and modulation of virus life cycle by host cell factors, to aid better design of vaccines.

Methodologically, we are developing a cellular tomography pipeline for direct visualization of virus-replication intermediates in their native environment, which can be widely applied to various biological systems and soft matters. Specifically, we will:

1) Develop a cryo-correlative light and electron microscopy (cryo-CLEM), cryo-FIB and cryo-ET pipeline to study the life cycle of virus and host-virus interactions in situ;

2) Incorporate Artificial Intelligence to aid high-throughput automated data collection and data analysis (such as biomolecules target recognition and heterogeneity analysis);

3) Develop subtomogram averaging methods to enable the large-scale and high-throughput macromolecule structure determination in subnanometer resolution in situ. 

1| Ni T*, Frosio T*, Mendonça L*, Sheng Y, Clare D, Himes BA, Zhang P. High-resolution in situ structure determination by cryo-electron tomography and subtomogram averaging using emClarity. Nat Protoc. 2022 Jan 12. doi: 10.1038/s41596-021-00648-5. PMID: 35022621.

2| Ni T*, Jiang Q*, Ng PC, Shen J, Dou H, Zhu Y, Radecke J, Dykes GF, Huang F, Liu LN, Zhang P. Intrinsically disordered CsoS2 acts as a general molecular thread for α-carboxysome shell assembly. Nat Commun. 2023 Sep 7;14(1):5512. doi: 10.1038/s41467-023-41211-y. PMID: 37679318; PMCID: PMC10484944.

3| Ni T*, Jiao F*, Yu X*, Aden S, Ginger L, Williams SI, Bai F, Pražák V, Karia D, Stansfeld P, Zhang P, Munson G, Anderluh G, Scheuring S, Gilbert RJC. Structure and mechanism of bactericidal mammalian perforin-2, an ancient agent of innate immunity. Sci Adv. 2020 Jan 29;6(5):eaax8286. doi: 10.1126/sciadv.aax8286. PMID: 32064340; PMCID: PMC6989145.

4| Ni T, Gerard S, Zhao G, Dent K, Ning J, Zhou J, Shi J, Anderson-Daniels J, Li W, Jang S, Engelman AN, Aiken C, Zhang P. Intrinsic curvature of the HIV-1 CA hexamer underlies capsid topology and interaction with cyclophilin A. Nat Struct Mol Biol. 2020 Sep;27(9):855-862. doi: 10.1038/s41594-020-0467-8. PMID: 32747784; PMCID: PMC8064030.

5| Ni T*, Zhu Y*, Yang Z*, Xu C, Chaban Y, Nesterova T, Ning J, Böcking T, Parker MW, Monnie C, Ahn J, Perilla JR, Zhang P. Structure of native HIV-1 cores and their interactions with IP6 and CypA. Sci Adv. 2021 Nov 19;7(47):eabj5715. doi: 10.1126/sciadv.abj5715. PMID: 34797722; PMCID: PMC8604400. 

Full publication list link:

https://www.tni-lab.org/publications/

 HKU-100 professoriate