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

PLoS Pathogens
Wenfei SongYe Xiang

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, ...Continue Reading

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Datasets Mentioned

BETA
EMD-9584
EMD-9583

Methods Mentioned

BETA
gel-filtration
size-exclusion chromatography
electrophoresis

Software Mentioned

ResMap
COOT
Gautomacth
ROSETTA
Gctf
Gautomatch
e2pdb2mrc
RELION
SWISS
UCSF Chimera

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