Gang Ye

TL;DR: This study determines the crystal structure of the receptor-binding domain (RBD) of the spike protein of SARS-CoV-2 (engineered to facilitate crystallization) in complex with ACE2 and sheds light on the structural features that increase its binding affinity to ACE2.

TL;DR: Key cell entry mechanisms of SARS-CoV-2 that potentially contribute to the immune evasion, cell infectivity, and wide spread of the virus are identified using biochemical and pseudovirus entry assays and the potency and evasiveness are highlighted.

TL;DR: The interactions between the S protein and its receptor porcine aminopeptidase N (pAPN) or co-receptor sugars are investigated, indicating that PEDV conforms to a different receptor recognition model compared with transmissible gastroenteritis virus (TGEV), porcines respiratory CoV, and human coronavirus NL63 (HCoV-NL63).

TL;DR: In this paper , the 3.0 Å cryo-EM structure of the omicron spike protein ectodomain was determined, and the stable open conformation of the spike molecules shed light on the cell entry and immune evasion mechanisms of the Omicron variant.

TL;DR: Four crystal structures are determined, including wild-type porcine delta coronavirus (PDCoV) nsp9, PDCoV nsp 9-ΔN7 (N-terminal 7 amino acids deleted), wild- type porcinespine epidemic diarrhea virus (PEDV) c9, and PEDV nSP9-C59A mutant, which reveal the diverse dimerization forms of coronaviruses.