EconPapers    
Economics at your fingertips  
 

Sequence signatures of two public antibody clonotypes that bind SARS-CoV-2 receptor binding domain

Timothy J. C. Tan, Meng Yuan, Kaylee Kuzelka, Gilberto C. Padron, Jacob R. Beal, Xin Chen, Yiquan Wang, Joel Rivera-Cardona, Xueyong Zhu, Beth M. Stadtmueller, Christopher B. Brooke, Ian A. Wilson () and Nicholas C. Wu ()
Additional contact information
Timothy J. C. Tan: University of Illinois at Urbana-Champaign
Meng Yuan: The Scripps Research Institute
Kaylee Kuzelka: University of Illinois at Urbana-Champaign
Gilberto C. Padron: University of Illinois at Urbana-Champaign
Jacob R. Beal: University of Illinois at Urbana-Champaign
Xin Chen: University of Illinois at Urbana-Champaign
Yiquan Wang: University of Illinois at Urbana-Champaign
Joel Rivera-Cardona: University of Illinois at Urbana-Champaign
Xueyong Zhu: The Scripps Research Institute
Beth M. Stadtmueller: University of Illinois at Urbana-Champaign
Christopher B. Brooke: University of Illinois at Urbana-Champaign
Ian A. Wilson: The Scripps Research Institute
Nicholas C. Wu: University of Illinois at Urbana-Champaign

Nature Communications, 2021, vol. 12, issue 1, 1-10

Abstract: 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.

Date: 2021
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-021-24123-7 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-24123-7

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-021-24123-7

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().

 
Page updated 2025-03-19
Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-24123-7