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Cryo-EM Structures of SARS-CoV-2 Spike without and with ACE2 Reveal a pH-Dependent Switch to Mediate Endosomal Positioning of Receptor-Binding Domains.
<div class='caption-title'>Cryo-EM Structures of SARS-CoV-2 Spike with ACE2 Show Similar Stoichiometries at Serological and Endosomal pH</div>
<div class='caption-title'>Coordinated Inter-Protomer Domain Movements Assist in Raising RBD to Bind ACE2</div>
Zhou T, Tsybovsky Y, Gorman J, Rapp M, Cerutti G, Chuang GY, Katsamba PS, Sampson JM, Schön A, Bimela J, Boyington JC, Nazzari A, Olia AS, Shi W, Sastry M, Stephens T, Stuckey J, Teng IT, Wang P, Wang S, Zhang B, Friesner RA, Ho DD, Mascola JR, Shapiro L, Kwong PD
OpenAccess logo Cell Host Microbe 28 867-879.e5 (2020)
Related entries: 6xlu, 6xm0, 6xm3, 6xm5, 7jwy, 7kmb, 7kms, 7kmz, 7knb, 7kne, 7knh, 7kni

Cited: 225 times
EuropePMC logo PMID: 33271067

Abstract

The SARS-CoV-2 spike employs mobile receptor-binding domains (RBDs) to engage the human ACE2 receptor and to facilitate virus entry, which can occur through low-pH-endosomal pathways. To understand how ACE2 binding and low pH affect spike conformation, we determined cryo-electron microscopy structures-at serological and endosomal pH-delineating spike recognition of up to three ACE2 molecules. RBDs freely adopted "up" conformations required for ACE2 interaction, primarily through RBD movement combined with smaller alterations in neighboring domains. In the absence of ACE2, single-RBD-up conformations dominated at pH 5.5, resolving into a solitary all-down conformation at lower pH. Notably, a pH-dependent refolding region (residues 824-858) at the spike-interdomain interface displayed dramatic structural rearrangements and mediated RBD positioning through coordinated movements of the entire trimer apex. These structures provide a foundation for understanding prefusion-spike mechanics governing endosomal entry; we suggest that the low pH all-down conformation potentially facilitates immune evasion from RBD-up binding antibody.

Reviews - 6xm4 mentioned but not cited (5)

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Articles - 6xm4 mentioned but not cited (26)

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Reviews citing this publication (39)

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Articles citing this publication (155)

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