literature

SARS_CoV_2 mutation literature information.

The SARS-CoV-2 B.1.618 variant slightly alters the spike RBD-ACE2 binding affinity and is an antibody escaping variant: a computational structural perspective.

PMID: 35480256 2021 RSC advances

Abstract: Our results revealed that the E484K mutation in the RBD slightly altered the binding affinity through affecting the hydrogen bonding network.

Abstract: The recently reported variant B.1.618, which possesses the E484K mutation specific to the receptor-binding domain (RBD), as well as two deletions of Tyr145 and His146 at the N-terminal binding domain (NTD) of the spike protein, must be studied in depth to devise new therapeutic options.

Thermodynamics and kinetics in antibody resistance of the 501Y.V2 SARS-CoV-2 variant.

PMID: 35497518 2021 RSC advances

Abstract: Three substitutions in the RBD including K417N, E484K, and N501Y alter the free energy landscape, binding pose, binding free energy, binding kinetics, hydrogen bonding, nonbonded contacts, and unbinding pathway of RBD + NAb complexes.

SARS-CoV-2 escape in vitro from a highly neutralizing COVID-19 convalescent plasma.

PMID: 33398278 2020 bioRxiv

Introduction: In contrast, the single mutation in the RBD (E484K) swaps the charge of the sidechain, which would significantly alter the electrostatic complementarity of antibody binding to this region.

Introduction: In the RBD, the possibility to escape is limited and the mutation E484K that we found is one of the most frequent mutations to escape monoclonal antibodies and among the most common RBD mutations described in experimental settings as well as in natural isolates posted in the GISAD database.

Introduction: The ability of the virus to adapt to the host immune system was also observed in clinical settings where an immunocompromised COVID-19 patient, after 154 days of infection, presented different variants of the virus including the

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