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Single-particle cryo-EM unaligned micrographs of neutralizing antibody 910-30 in complex with SARS-CoV-2 spike glycoprotein (disrupted form)

ABSTRACT:

SUBMITTER: Gabriele Cerutti 

PROVIDER: EMPIAR-11913 | biostudies-other |

REPOSITORIES: biostudies-other

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Paired heavy- and light-chain signatures contribute to potent SARS-CoV-2 neutralization in public antibody responses.

Banach Bailey B BB   Cerutti Gabriele G   Fahad Ahmed S AS   Shen Chen-Hsiang CH   Oliveira De Souza Matheus M   Katsamba Phinikoula S PS   Tsybovsky Yaroslav Y   Wang Pengfei P   Nair Manoj S MS   Huang Yaoxing Y   Francino-Urdániz Irene M IM   Steiner Paul J PJ   Gutiérrez-González Matías M   Liu Lihong L   Liu Lihong L   López Acevedo Sheila N SN   Nazzari Alexandra F AF   Wolfe Jacy R JR   Luo Yang Y   Olia Adam S AS   Teng I-Ting IT   Yu Jian J   Zhou Tongqing T   Reddem Eswar R ER   Bimela Jude J   Pan Xiaoli X   Madan Bharat B   Laflin Amy D AD   Nimrania Rajani R   Yuen Kwok-Yung KY   Whitehead Timothy A TA   Ho David D DD   Kwong Peter D PD   Shapiro Lawrence L   DeKosky Brandon J BJ  

Cell reports 20210928 1

Understanding mechanisms of protective antibody recognition can inform vaccine and therapeutic strategies against SARS-CoV-2. We report a monoclonal antibody, 910-30, targeting the SARS-CoV-2 receptor-binding site for ACE2 as a member of a public antibody response encoded by IGHV3-53/IGHV3-66 genes. Sequence and structural analyses of 910-30 and related antibodies explore how class recognition features correlate with SARS-CoV-2 neutralization. Cryo-EM structures of 910-30 bound to the SARS-CoV-2  ...[more]

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