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In a new study, researchers used a cell-cell fusion assay to extract potentially cleaved spike protein products from syncytia in order to explore the functional and biochemical characteristics of spike (S) protein when it engages its receptor ACE2 in living cells.
An interesting preprint research paper describes structural changes resulting from the multiple mutations found in the recent Omicron variant of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). SARS-CoV-2 is the causative agent behind the coronavirus disease 2019 (COVID-19) pandemic. In addition, the research describes the consequent effects of these changes on Omicron’s infectivity and immune evasion capabilities.
New study findings show that the clinical-grade soluble ACE2 effectively inhibits the SARS-CoV-2 Omicron variant, which proves the principle of an effective therapeutic approach against Omicron-driven COVID-19 infections.
Now in new research, scientists from the University of Leicester have been investigating how these mutations alter the affinities of RBDs to ACE2.
A new study highlights the potential evolutionary trade-off observed in the omicron variant, detailing the dynamics of the protein structure, its interactions, and subsequent effects.