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TitlePaired heavy- and light-chain signatures contribute to potent SARS-CoV-2 neutralization in public antibody responses.
Journal, issue, pagesCell Rep, Vol. 37, Issue 1, Page 109771, Year 2021
Publish dateOct 5, 2021
AuthorsBailey B Banach / Gabriele Cerutti / Ahmed S Fahad / Chen-Hsiang Shen / Matheus Oliveira De Souza / Phinikoula S Katsamba / Yaroslav Tsybovsky / Pengfei Wang / Manoj S Nair / Yaoxing Huang / Irene M Francino-Urdániz / Paul J Steiner / Matías Gutiérrez-González / Lihong Liu / Sheila N López Acevedo / Alexandra F Nazzari / Jacy R Wolfe / Yang Luo / Adam S Olia / I-Ting Teng / Jian Yu / Tongqing Zhou / Eswar R Reddem / Jude Bimela / Xiaoli Pan / Bharat Madan / Amy D Laflin / Rajani Nimrania / Kwok-Yung Yuen / Timothy A Whitehead / David D Ho / Peter D Kwong / Lawrence Shapiro / Brandon J DeKosky /
PubMed AbstractUnderstanding 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 ...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 spike trimer reveal binding interactions and its ability to disassemble spike. Despite heavy-chain sequence similarity, biophysical analyses of IGHV3-53/3-66-encoded antibodies highlight the importance of native heavy:light pairings for ACE2-binding competition and SARS-CoV-2 neutralization. We develop paired heavy:light class sequence signatures and determine antibody precursor prevalence to be ∼1 in 44,000 human B cells, consistent with public antibody identification in several convalescent COVID-19 patients. These class signatures reveal genetic, structural, and functional immune features that are helpful in accelerating antibody-based medical interventions for SARS-CoV-2.
External linksCell Rep / PubMed:34587480 / PubMed Central
MethodsEM (single particle)
Resolution4.75 - 5.78 Å
Structure data

23016

7ks9

EMDB-23016, PDB-7ks9:
Cryo-EM structure of prefusion SARS-CoV-2 spike glycoprotein in complex with 910-30 Fab
Method: EM (single particle) / Resolution: 4.75 Å

EMDB-23039:
Cryo-EM map of SARS-CoV-2 spike glycoprotein in complex with 910-30 Fab (disrupted form)
Method: EM (single particle) / Resolution: 5.78 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • homo sapiens (human)
  • severe acute respiratory syndrome coronavirus 2
KeywordsViral Protein/IMMUNE SYSTEM / Neutralizing antibody / Fusion protein / Spike glycoprotein / COVID-19 / RBD / Viral protein / IMMUNE SYSTEM / Viral Protein-IMMUNE SYSTEM complex

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