Global emergencies caused by the severe acute respiratory syndrome coronavirus (SARS-CoV), Middle-East respiratory syndrome coronavirus (MERS-CoV) and SARS-CoV-2 significantly endanger human health. The spike (S) glycoprotein is the key antigen and its conserved S2 subunit contributes to viral entry by mediating host-viral membrane fusion. However, structural information of the post-fusion S2 from these highly pathogenic human-infecting coronaviruses is still lacking. We used single-particle cryo-electron microscopy to show that the post-fusion SARS-CoV S2 forms a further rotated HR1-HR2 six-helix bundle and a tightly bound linker region upstream of the HR2 motif. The structures of pre- and post-fusion SARS-CoV S glycoprotein dramatically differ, resembling that of the Mouse hepatitis virus (MHV) and other class I viral fusion proteins. This structure suggests potential targets for the development of vaccines and therapies against a wide range of SARS-like coronaviruses. The spike (S) protein of coronaviruses is responsible for receptor recognition and the fusion between the viral membrane and the of cell host membrane. Here the authors report a cryo-EM structure of SARS-CoV post-fusion S2 trimer, providing insights into the fusion mechanism that could be useful for therapeutic development against coronaviruses.
【저자키워드】 SARS virus, Cryoelectron microscopy, 【초록키워드】 Structure, SARS-CoV-2, Coronaviruses, Vaccine, coronavirus, therapy, SARS-CoV, Cryo-electron microscopy, Proteins, virus, MERS-CoV, viral entry, Antigen, Protein, Health, Hepatitis, therapeutic, membrane, target, membrane fusion, glycoprotein, receptor, mouse, information, MHV, mechanism, S2 subunit, acute respiratory syndrome, viral membrane, SARS-like coronaviruses, trimer, respiratory syndrome coronavirus, motif, upstream, highly pathogenic, SARS-CoV S, Host, cryo-EM structure, Cell, linker, responsible, caused, conserved, significantly, form, contribute, 【제목키워드】 SARS-CoV, spike glycoprotein, Analysis,