Xinquan Wang

TL;DR: High-resolution crystal structures of the receptor-binding domain of the spike protein of SARS-CoV-2 and SARS -CoV in complex with ACE2 provide insights into the binding mode of these coronaviruses and highlight essential ACE2-interacting residues.

TL;DR: In this paper, two new components of the human m6A methyltransferase complex, Wilms' tumor 1-associating protein (WTAP) and methyl transferase like 14 (METTL14), were reported.

TL;DR: In a study of antibodies isolated from patients infected with SARS-CoV-2, antibodies that potently neutralized the virus competed with angiotensin-converting enzyme 2 for binding to the receptor-binding domain of the viral spike protein, suggesting that antibodies that disrupt this interaction could be developed to treat Sars-Cov-2 infection.

TL;DR: Structural comparisons suggested that the SARS-CoV S glycoprotein retains a prefusion architecture after trypsin cleavage into the S1 and S2 subunits and acidic pH treatment, however, binding to the receptor opens up the receptor-binding domain of S1, which could promote the release of the S 1-ACE2 complex and S1 monomers from the prefusion spike and trigger the pre- to postfusion conformational transition.

TL;DR: The atomic details at the interface between MERS-CoV RBD and DPP4 provide structural understanding of the virus and receptor interaction, which can guide development of therapeutics and vaccines against MERS -CoV infection.