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Cryo-EM structure of SARS-CoV-2 spike at pH 4.0

ABSTRACT:

SUBMITTER: Sergei Pletnev

PROVIDER: EMPIAR-10723 | biostudies-other |

REPOSITORIES: biostudies-other

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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.

Zhou Tongqing T Tsybovsky Yaroslav Y Gorman Jason J Rapp Micah M Cerutti Gabriele G Chuang Gwo-Yu GY Katsamba Phinikoula S PS Sampson Jared M JM Schön Arne A Bimela Jude J Boyington Jeffrey C JC Nazzari Alexandra A Olia Adam S AS Shi Wei W Sastry Mallika M Stephens Tyler T Stuckey Jonathan J Teng I-Ting IT Wang Pengfei P Wang Shuishu S Zhang Baoshan B Friesner Richard A RA Ho David D DD Mascola John R JR Shapiro Lawrence L Kwong Peter D PD

Cell host & microbe 20201117 6

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 com ...[more]

PMID: 33271067

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