Yaning Li

TL;DR: In this paper, the bivalent binding of the full-length IgG is found to associate with more RBDs in the "up" conformation than the monovalent binding of Fab, perhaps contributing to the enhanced neutralizing activity of IgG and triggering more shedding of the S1 subunit from the S protein.

TL;DR: Results revealed that ADE mediated by SARS-CoV-2 spike-specific antibodies could result from binding to the receptor in slightly different pattern from antibodies mediating neutralizations, which could be of use for developing novel therapeutic and preventive measures for control of COVID-19 infection.

TL;DR: In this paper, a human angiotensin-converting enzyme 2 (ACE2)-targeting monoclonal antibody, 3E8, blocked the S1-subunits and pseudo-typed virus constructs from multiple coronaviruses including SARS-CoV-2, SARS CoV-1, HCoVNL63, B.1.1, and P.617, without markedly affecting the physiological activities of ACE2 or causing severe toxicity.

TL;DR: In this paper, the sterol regulatory element-binding protein (SREBP) pathway was analyzed in the presence of 25-hydroxycholesterol (25HC)-dependent association of Scap and Insig acts as the master switch for the SREBP pathway.

TL;DR: Cryo-EM structures of the ten most potent nAbs in their native full-length IgG or Fab forms bound to the trimeric S protein of SARS-CoV-2 reveal the bivalent binding and their correlation with more potent neutralization and the shedding of S1 subunit.