Tetherin downregulation by SARS-CoV-2 enhances viral spread
A new preprint research paper published on the bioRxiv server describes the role of a host protein called tetherin in the spread of the novel coronavirus.
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A new preprint research paper published on the bioRxiv server describes the role of a host protein called tetherin in the spread of the novel coronavirus.
An interesting new study published on the bioRxiv preprint server describes a new platform that allows a high-throughput workflow to generate matched human lung buds in the tens of thousands. This allows researchers to study SARS-CoV-2 infection and therapeutics in lung tissue that mirrors the key aspects of human lung development.
In a recent and timely paper, currently available on the bioRxiv preprint server, researchers from Israel and France demonstrated how in vitro evolution of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) receptor-binding domain (RBD) follows contagious mutation spread – but can also generate an efficient infection inhibitor.
A recent study has found that extracellular vimentin can bind to SARS-CoV-2 spike protein in vitro, and antibodies against vimentin can decrease virus infectivity by up to 80%. This suggests vimentin could aid the virus’s binding to host cells and help in infection.
Potential treatment approach to new COVID-19 variant Researchers in the United States have demonstrated a potential new approach to treating infection with the new variant of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) – the agent that causes coronavirus disease 2019 (COVID-19). The team used all-atom molecular dynamics to explore the mechanisms underlying the increased infectivity and spread of the recently emerged B.1.1.7 lineage that has been designated a variant of concern by Public Health England. The researchers showed that a mutation within B.1.1.7 increases the viru...