Cellular Mechanisms for TIM Protein-Assisted Viral Adhesion and Entry

Overview

Lehigh University Virus infections pose significant global health, economic and social challenges, especially with the emergence of new resistant viral strains like Ebola and Corona. Mechanistic understanding and characterization of how viruses manipulate our cells during the initial attachment in the cellular adhesion process is critical to slow down the infection and develop effective anti-viral therapies for treatments. Introduction of small molecules or functionalized nanoparticles as bioactive agents to neutralize virus ligand domains or adhesion receptors before the viral entry has created an opportunity to customize and enhance the therapeutic efficacy of anti-viral treatments. This research focuses on developing a meso-scale coarse-grained mechanistic model and conducting three- dimensional dynamic simulations to characterize the interactions of the virus as it approaches the host cells. T-cell Immunoglobulin-Mucin (TIM) family of protein receptors play a vital role in cellular adhesion and viral entry by binding with phosphatidylserine (PS) domains on the virus surface. Reducing receptor density or strength of interactions with virions can be effective in slowing down the attachment process. Simulations show that increase in temperature makes adhesion harder and eventually leads to complete detachment of virions. Inducing a bit of tension in the membrane can compensate for thermal fluctuations, however, further increase in osmotic tension will impede the viral attachment. Spherical virions take longer to attach compared to the cylindrical virions, confirming the importance of size and shape effects. This was leveraged in demonstrating the potential of functionalized nanoparticles as sizeselective inhibitors for reducing risk of infection against a specific family of viruses. Cooperative Relaxation in Supercooled Liquids: Kadanoff’s Block Construction and Wilson’s Renormalization Group Transformation Nadine Meister (3rd Place Chemistry) Centennial High School Ellicott City, Maryland Dr. Udayan Mohanty Boston College The relaxation time of supercooled liquids diverges as the temperature approaches the Kauzmann temperature. The Adam-Gibbs model of relaxation in supercooled liquids relates the relaxation time to the configurational entropy by introducing the idea of cooperatively rearranging regions. We developed the renormalization group transformation by decreasing degrees of freedom and increasing scale length of the cooperatively rearranging regions. The fixed point of the transformation is determined and the Adam-Gibbs relationship between size of rearranging regions and entropy emerges, explaining the non-analytic behavior of relaxation time at the Kauzmann temperature. The renormalization group transformations provide new insights on the universality of Adam-Gibbs’ relationship of different liquids as they all start from the ridgeline of the renormalization group manifold and converge to the same fixed point. Finally, we predict the configurational fraction for certain polymer liquids. This work provides an unexpected route explaining how kinetics and thermodynamic properties are related to the molecular motions of these glass-forming liquids, as well as fueling developments in real life applications.

Competition history

• JSHS 2020 Category not listed

Resources

• National JSHS abstract book ↗

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