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3 results on '"Kaylee Kuzelka"'

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

Author

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

Subjects
Science
Abstract

Public antibody clonotypes that recognize SARS-CoV-2 spike protein are important for protection against COVID-19. Here, the authors characterize sequence motifs in the heavy chain complementarity-determining region (CDR) H3s of two public clonotypes and their association with light chain identity.

Published
2021
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2. Sequence signatures of two public antibody clonotypes that bind SARS-CoV-2 receptor binding domain

Author

Nicholas C. Wu, Gilberto C. Padron, Xueyong Zhu, Kaylee Kuzelka, Jacob R. Beal, Yiquan Wang, Beth M. Stadtmueller, Xin Chen, Ian A. Wilson, Timothy J. C. Tan, Meng Yuan, Joel Rivera-Cardona, and Christopher B. Brooke

Subjects
0301 basic medicine, Models, Molecular, Science, Protein domain, General Physics and Astronomy, Somatic hypermutation, Plasma protein binding, Immunoglobulin light chain, Crystallography, X-Ray, General Biochemistry, Genetics and Molecular Biology, Antibodies, Article, 03 medical and health sciences, 0302 clinical medicine, Protein Domains, Humans, Amino Acid Sequence, Peptide sequence, Binding selectivity, X-ray crystallography, Genetics, Multidisciplinary, biology, SARS-CoV-2, COVID-19, High-Throughput Nucleotide Sequencing, General Chemistry, Antibodies, Neutralizing, Complementarity Determining Regions, 030104 developmental biology, Antibody Formation, Spike Glycoprotein, Coronavirus, biology.protein, Angiotensin-Converting Enzyme 2, Antibody, Sequence motif, 030217 neurology & neurosurgery, Protein Binding
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., Public antibody clonotypes that recognize SARS-CoV-2 spike protein are important for protection against COVID-19. Here, the authors characterize sequence motifs in the heavy chain complementarity-determining region (CDR) H3s of two public clonotypes and their association with light chain identity.

Published
2021

3. Sequence signatures of two IGHV3-53/3-66 public clonotypes to SARS-CoV-2 receptor binding domain

Author

Nicholas C. Wu, Jacob R. Beal, Meng Yuan, Ian A. Wilson, Gilberto C. Padron, Yiquan Wang, Timothy J. C. Tan, Beth M. Stadtmueller, Joel Rivera-Cardona, Xueyong Zhu, Xin Chen, Kaylee Kuzelka, and Christopher B. Brooke

Subjects
biology, Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), biology.protein, medicine, Somatic hypermutation, Computational biology, Antibody, Immunoglobulin light chain, Sequence motif, medicine.disease_cause, Binding selectivity, Sequence (medicine), Coronavirus
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 CDR H3. Germline-encoded sequence motifs in CDRs H1 and H2 play a major role, but whether any common motifs are present in CDR H3, which is often critical for binding specificity, have not been elucidated. 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 appear 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. Overall, our results advance fundamental understanding of the antibody response to SARS-CoV-2.

Published
2021

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