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Sequence signatures of two public antibody clonotypes that bind SARS-CoV-2 receptor binding domain.
Tan, Timothy J C; Yuan, Meng; Kuzelka, Kaylee; Padron, Gilberto C; Beal, Jacob R; Chen, Xin; Wang, Yiquan; Rivera-Cardona, Joel; Zhu, Xueyong; Stadtmueller, Beth M; Brooke, Christopher B; Wilson, Ian A; Wu, Nicholas C.
  • Tan TJC; Center for Biophysics and Quantitative Biology, University of Illinois at Urbana-Champaign, Urbana, IL, USA.
  • Yuan M; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, USA.
  • Kuzelka K; Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL, USA.
  • Padron GC; Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL, USA.
  • Beal JR; Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL, USA.
  • Chen X; Center for Biophysics and Quantitative Biology, University of Illinois at Urbana-Champaign, Urbana, IL, USA.
  • Wang Y; Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL, USA.
  • Rivera-Cardona J; Department of Microbiology, University of Illinois at Urbana-Champaign, Urbana, IL, USA.
  • Zhu X; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, USA.
  • Stadtmueller BM; Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL, USA.
  • Brooke CB; Department of Microbiology, University of Illinois at Urbana-Champaign, Urbana, IL, USA.
  • Wilson IA; Carl R. Woese Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, IL, USA.
  • Wu NC; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, USA. wilson@scripps.edu.
Nat Commun ; 12(1): 3815, 2021 06 21.
Article in English | MEDLINE | ID: covidwho-1279879
ABSTRACT
Since the COVID-19 pandemic onset, the antibody response to SARS-CoV-2 has been extensively characterized. Antibodies to the receptor binding domain (RBD) on the spike protein are frequently encoded by IGHV3-53/3-66 with a short complementarity-determining region (CDR) H3. Germline-encoded sequence motifs in heavy chain CDRs H1 and H2 have a major function, but whether any common motifs are present in CDR H3, which is often critical for binding specificity, is not clear. Here, we identify two public clonotypes of IGHV3-53/3-66 RBD antibodies with a 9-residue CDR H3 that pair with different light chains. Distinct sequence motifs on CDR H3 are present in the two public clonotypes that seem to be related to differential light chain pairing. Additionally, we show that Y58F is a common somatic hypermutation that results in increased binding affinity of IGHV3-53/3-66 RBD antibodies with a short CDR H3. These results advance understanding of the antibody response to SARS-CoV-2.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Antibodies, Neutralizing / Spike Glycoprotein, Coronavirus / Angiotensin-Converting Enzyme 2 / SARS-CoV-2 / COVID-19 Limits: Humans Language: English Journal: Nat Commun Journal subject: Biology / Science Year: 2021 Document Type: Article Affiliation country: S41467-021-24123-7

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Antibodies, Neutralizing / Spike Glycoprotein, Coronavirus / Angiotensin-Converting Enzyme 2 / SARS-CoV-2 / COVID-19 Limits: Humans Language: English Journal: Nat Commun Journal subject: Biology / Science Year: 2021 Document Type: Article Affiliation country: S41467-021-24123-7