Dataset Information


Cryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2.

ABSTRACT: The trimeric SARS coronavirus (SARS-CoV) surface spike (S) glycoprotein consisting of three S1-S2 heterodimers binds the cellular receptor angiotensin-converting enzyme 2 (ACE2) and mediates fusion of the viral and cellular membranes through a pre- to postfusion conformation transition. Here, we report the structure of the SARS-CoV S glycoprotein in complex with its host cell receptor ACE2 revealed by cryo-electron microscopy (cryo-EM). The complex structure shows that only one receptor-binding domain of the trimeric S glycoprotein binds ACE2 and adopts a protruding "up" conformation. In addition, we studied the structures of the SARS-CoV S glycoprotein and its complexes with ACE2 in different in vitro conditions, which may mimic different conformational states of the S glycoprotein during virus entry. Disassociation of the S1-ACE2 complex from some of the prefusion spikes was observed and characterized. We also characterized the rosette-like structures of the clustered SARS-CoV S2 trimers in the postfusion state observed on electron micrographs. 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 S1-ACE2 complex and S1 monomers from the prefusion spike and trigger the pre- to postfusion conformational transition.


PROVIDER: S-EPMC6107290 | BioStudies | 2018-01-01

REPOSITORIES: biostudies

Similar Datasets

2020-01-01 | S-EPMC7775788 | BioStudies
2018-01-01 | S-EPMC6200764 | BioStudies
2009-01-01 | S-EPMC2794128 | BioStudies
2020-01-01 | S-EPMC7557167 | BioStudies
2020-01-01 | S-EPMC7464562 | BioStudies
2004-01-01 | S-EPMC7092904 | BioStudies
2021-01-01 | S-EPMC7829931 | BioStudies
2020-01-01 | S-EPMC7319274 | BioStudies
2020-01-01 | S-EPMC7102599 | BioStudies
2020-01-01 | S-EPMC7347485 | BioStudies