Corpus overview


MeSH Disease

HGNC Genes

SARS-CoV-2 proteins

ProteinS (2)


SARS-CoV-2 Proteins
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    Molecular basis for a germline-biased neutralizing antibody response to SARS-CoV-2

    Authors: Sarah Ashley Clark; Lars Eric Clark; Adrian Coscia; Lindsay G.A. McKay; Sundaresh Shankar; Rebecca I. Johnson; Anthony Griffiths; Jonathan Abraham; Christophe Buyck; Johan Neyts; Marnix Van Loock; Leo James; Jakob luptak; Guinevere L Grice; Soraya Ebrahimi; Xiaoli Xiong; John AG Briggs; Sumita Pai; angalee nadesalingham; Marie-Christine Ouellet; Marc-André Roy; Marie-Christine Saint-Jacques; Claudia Savard

    doi:10.1101/2020.11.13.381533 Date: 2020-11-13 Source: bioRxiv

    The SARS-CoV-2 viral spike (S) protein PROTEIN mediates attachment and entry into host cells and is a major target of vaccine and drug design. Potent SARS-CoV-2 neutralizing antibodies derived from closely related antibody heavy chain genes ( IGHV3-53 HGNC or 3-66) have been isolated from multiple COVID-19 MESHD convalescent individuals. These usually contain minimal somatic mutations and bind the S receptor-binding domain (RBD) to interfere with attachment to the cellular receptor angiotensin-converting enzyme 2 ( ACE2 HGNC). We used antigen-specific single B cell sorting to isolate S-reactive monoclonal antibodies from the blood of a COVID-19 MESHD convalescent individual. The seven most potent neutralizing antibodies were somatic variants of the same IGHV3-53 HGNC-derived antibody and bind the RBD with varying affinity. We report X-ray crystal structures of four Fab HGNC variants bound to the RBD and use the structures to explain the basis for changes in RBD affinity. We show that a germline revertant antibody binds tightly to the SARS-CoV-2 RBD MESHD and neutralizes virus, and that gains in affinity for the RBD do not necessarily correlate with increased neutralization potency, suggesting that somatic mutation is not required to exert robust antiviral effect. Our studies clarify the molecular basis for a heavily germline-biased human antibody response to SARS-CoV-2.

    An alternative binding mode of IGHV3-53 HGNC antibodies to the SARS-CoV-2 receptor binding domain

    Authors: Nicholas C. Wu; Meng Yuan; Hejun Liu; Chang-Chun D. Lee; Xueyong Zhu; Sandhya Bangaru; Jonathan L. Torres; Tom G. Caniels; Philip J.M. Brouwer; Marit J. van Gils; Rogier W. Sanders; Andrew B. Ward; Ian A. Wilson

    doi:10.1101/2020.07.26.222232 Date: 2020-07-27 Source: bioRxiv

    IGHV3-53 HGNC-encoded neutralizing antibodies are commonly elicited during SARS-CoV-2 infection MESHD and target the receptor-binding domain (RBD) of the spike (S) protein PROTEIN. Such IGHV3-53 HGNC antibodies generally have a short CDR H3 due to structural constraints in binding the RBD (mode A). However, a small subset of IGHV3-53 HGNC antibodies to the RBD contain a longer CDR H3. Crystal structures of two IGHV3-53 HGNC 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 HGNC 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 HGNC in this common antibody response to SARS-CoV-2, where conserved IGHV3-53 HGNC germline-encoded features can be combined with very different CDR H3 lengths and light chains for SARS-CoV-2 RBD MESHD recognition and virus neutralization.

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MeSH Disease
HGNC Genes
SARS-CoV-2 Proteins

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