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Cleavage site recognition by SARS-CoV-2 main protease as new antiviral drug target

Cleavage site recognition by SARS-CoV-2 main protease as new antiviral drug target The main protease of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) cleaves the proteins produced by the virus at various stages of replication and maturation. Highly conserved across coronaviruses due to the essential functional role of the enzyme, it also makes an appealing drug target. Many research groups have and are investigating main protease inhibitors as antiviral drugs, and in a paper recently uploaded to the bioRxiv preprint server, a team of researchers examine the crystal structure of the protein while bound to various viral substrate peptides (P1-4). In doing so, they reveal the way in which the bound peptide sequence can direct and modulate enzyme activity, providing new templates towards antiviral drug design.

Double Mutant Variant In India Shouldn t Really Be Called That, Scientists Say : Goats and Soda : NPR

Like all viruses, the coronavirus mutates. Above: In this depiction of the the South African coronavirus variant B.1.531, the thin yellow band around the rim of indicates a mutation site. The virus spike (red) is attaching to a human cell receptor (blue). Juan Gaertner India is in the midst of a devastating second wave of COVID-19. For the past several weeks, cases and deaths have skyrocketed. The country is recording more than a quarter million cases per day. The situation in India sounds remarkably similar to what has happened in Brazil, South Africa and now also Iran, says infectious disease scientist Kristian Andersen at Scripps Research Institute. These countries already had a lot of people infected [in the first wave], and there was a sense that the country had reached some level of herd immunity, he says. But then, over time, as people s immunity waned, more contagious variants came along and sparked another surge.

Researchers provide ultrastructural details of SARS-CoV-2-infected respiratory epithelial cells

Researchers provide ultrastructural details of SARS-CoV-2-infected respiratory epithelial cells A team of scientists from the United Kingdom recently investigated the ultrastructural details of the attachment, entry, and budding processes of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) in the human airway epithelium. They have used a highly differentiated air-liquid interface cultures of airway epithelium to thoroughly investigate the viral infection cycle. The study is currently available on the Background SARS-CoV-2, the causative pathogen of coronavirus disease 2019 (COVID-19), is an enveloped RNA virus belonging to the Coronaviridae family. The virus primarily attacks human airway epithelial cells to initiate infection. Mechanistically, the receptor-binding domain (RBD) of the S1 subunit of the viral spike glycoprotein binds to angiotensin-converting enzyme 2 (ACE2), which is ubiquitously expressed at the apical surface of host airway epithelial cells. This is

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