Authors:

Guadalupe Lauro

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About Paper:

Coronaviruses have driven the last three pandemics, posing a major global health threat. A critical step in viral emergence is the ability to bind the proper host protein for it to enter the cell. For coronaviruses, the viral Spike protein's S1 domain binds to the human ACE2 receptor. Screening initial protein interactions across emerging coronaviruses can help predict potential outbreaks and guide early detection. We can predict how emerging coronaviruses do this by using computational methods to dock the proteins and analyze how sequence and structural differences influence binding. We predicted protein interactions using docking programs to screen how and where the two proteins may bind. Known pandemic coronaviruses served as controls to threshold emergents' behavior. Sequence and structural alignments identified conserved residues that informed how we guided the protein docking. Preliminary results show that across the emergents, sequence similarity ranges from 60-95% across the S1 domain. However, this range of differences is not reflected in structure. Structural alignments reveal the secondary structure is conserved with some differences in beta strands and disordered regions. Along with experimental data, these predictions aim to deepen our understanding of how binding mechanisms and protein conservation may contribute to human infection. Waterborne Dispersal Overwhelms Direct Contact as a Mechanism Of Seagrass Wasting Disease Transmission Alessandra Lawson

Source:

UC Davis / Microbiology & Molec Genetics / 2025

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Co-authors:

Guadalupe Lauro