Unknown

Dataset Information

0

An Alternative Binding Mode of IGHV3-53 Antibodies to the SARS-CoV-2 Receptor Binding Domain.

ABSTRACT: IGHV3-53-encoded neutralizing antibodies are commonly elicited during SARS-CoV-2 infection and target the receptor-binding domain (RBD) of the spike (S) protein. Such IGHV3-53 antibodies generally have a short CDR H3 because of structural constraints in binding the RBD (mode A). However, a small subset of IGHV3-53 antibodies to the RBD contain a longer CDR H3. Crystal structures of two IGHV3-53 neutralizing antibodies here demonstrate that a longer CDR H3 can be accommodated in a different binding mode (mode B). These two classes of IGHV3-53 antibodies both target the ACE2 receptor binding site, but with very different angles of approach and molecular interactions. Overall, these findings emphasize the versatility of IGHV3-53 in this common antibody response to SARS-CoV-2, where conserved IGHV3-53 germline-encoded features can be combined with very different CDR H3 lengths and light chains for SARS-CoV-2 RBD recognition and virus neutralization.

SUBMITTER: Wu NC 

PROVIDER: S-EPMC7522650 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

IGHV3-53-encoded neutralizing antibodies are commonly elicited during SARS-CoV-2 infection and target the receptor-binding domain (RBD) of the spike (S) protein. Such IGHV3-53 antibodies generally have a short CDR H3 because of structural constraints in binding the RBD (mode A). However, a small subset of IGHV3-53 antibodies to the RBD contain a longer CDR H3. Crystal structures of two IGHV3-53 neutralizing antibodies here demonstrate that a longer CDR H3 can be accommodated in a different bindi  ...[more]

Similar Datasets

Unknown Sequence signatures of two IGHV3-53/3-66 public clonotypes to SARS-CoV-2 receptor binding domain.
| S-EPMC7852275 | biostudies-literature
Unknown The prominent role of a CDR1 somatic hypermutation for convergent IGHV3-53/3-66 antibodies in binding to SARS-CoV-2.
| S-EPMC9045774 | biostudies-literature
Unknown Receptor-binding domain-specific human neutralizing monoclonal antibodies against SARS-CoV and SARS-CoV-2.
| S-EPMC7506210 | biostudies-literature
Unknown Potent and protective IGHV3-53/3-66 public antibodies and their shared escape mutant on the spike of SARS-CoV-2.
| S-EPMC8270942 | biostudies-literature
Unknown Recognition of the SARS-CoV-2 receptor binding domain by neutralizing antibodies.
| S-EPMC7547570 | biostudies-literature
Unknown Induction of IGHV3-53 public antibodies with broadly neutralising activity against SARS-CoV-2 including Omicron subvariants in a Delta breakthrough infection case.
| S-EPMC11565539 | biostudies-literature
Unknown Humanized single domain antibodies neutralize SARS-CoV-2 by targeting the spike receptor binding domain.
| S-EPMC7483421 | biostudies-literature
Unknown Neutralization of SARS-CoV-2 requires antibodies against conformational receptor-binding domain epitopes.
| S-EPMC8653362 | biostudies-literature
Unknown A Structural Landscape of Neutralizing Antibodies Against SARS-CoV-2 Receptor Binding Domain.
| S-EPMC8113771 | biostudies-literature
Unknown SARS-COV-2 recombinant Receptor-Binding-Domain (RBD) induces neutralizing antibodies against variant strains of SARS-CoV-2 and SARS-CoV-1.
| S-EPMC8387217 | biostudies-literature