The virus-host interactions on a nanoscale. 

The lab studies the molecular mechanisms underlying the transmission of zoonotic viruses among cells and the hosts’ restriction by combining super-resolution microscopy, fluorescence tool, and classic molecular cell biology approaches. Specifically, I am interested in the highly pathogenic, bat-borne zoonotic paramyxoviruses, such as Nipah (NiV) and Hendra (HeV) viruses, which belong to the henipavirus genus. We combine super-resolution imaging, new fluorescence tools, and classical molecular biology tools to probe the nanoscale organization and dynamics of virus-host complexes at physiological and disturbed conditions, aiming to reveal previously inaccessible structural and dynamic details in virus transmission and host response. 

Theme I: Paramyxovirus assembly and release. The assembly and release of paramyxovirus occur at the plasma membrane and are prerequisites for virus transmission. Despite decades of research, it remains unclear how viral proteins coordinate their assembly and how they interact with the plasma membrane and cortical actin to drive budding and release. By quantitatively analyzing the protein organization and dynamics at the individual virus assembly sites, we investigate the assembly and budding processes and identify host factors involved in these stages. Articles related to this theme are: Wang J. et al, Science Advances, 2025; Liu, QT. et al. Biophysical Journal, 2022; and Liu, Q et al., Nature Communications, 2018. 

Theme II: Henipavirus-induced membrane fusion and IFITM restriction.  Henipaviruses enter at the cell surface by fusing the virus and cell membranes. Henipaviruses employ multiple factors to gain cell entry: the receptor-binding protein and membrane fusion protein. Interferon-induced transmembrane (IFITM) proteins are innate immune factors that inhibit the entry of paramyxoviruses and other enveloped viruses by increasing the rigidity of viral and host cell membranes and/or by interacting directly with viral glycoproteins. Our current research focuses on elucidating how multiple host and viral factors coordinate to trigger virus entry and membrane fusion, and how host IFITM proteins regulate henipavirus entry. Currently, we address these questions by using single-molecule imaging to quantitatively analyze the organization and dynamics of the viral fusion machinery and the cell’s restriction proteins.  Articles related to this theme are: Wang Q. et al., eLife, 2025. 

Theme III: Single-molecule imaging technology development. We  build super-resolution microscopy imaging systems that offer versatile capabilities, including Total Internal Reflection Microscopy, single-molecule localization (SMLM), and single-molecule tracking (SMT). The custom-built system achieves a spatial resolution of 10 nm in a whole cell, outperforming currently available commercial super-resolution systems. We also develop algorithms to extract detailed information on the protein nanoscale organization and dynamics.