Dataset Information

Antibody escape and global spread of SARS-CoV-2 lineage A.27.

ABSTRACT: In spring 2021, an increasing number of infections was observed caused by the hitherto rarely described SARS-CoV-2 variant A.27 in south-west Germany. From December 2020 to June 2021 this lineage has been detected in 31 countries. Phylogeographic analyses of A.27 sequences obtained from national and international databases reveal a global spread of this lineage through multiple introductions from its inferred origin in Western Africa. Variant A.27 is characterized by a mutational pattern in the spike gene that includes the L18F, L452R and N501Y spike amino acid substitutions found in various variants of concern but lacks the globally dominant D614G. Neutralization assays demonstrate an escape of A.27 from convalescent and vaccine-elicited antibody-mediated immunity. Moreover, the therapeutic monoclonal antibody Bamlanivimab and partially the REGN-COV2 cocktail fail to block infection by A.27. Our data emphasize the need for continued global monitoring of novel lineages because of the independent evolution of new escape mutations.

SUBMITTER: Kaleta T

PROVIDER: S-EPMC8894356 | biostudies-literature | 2022 Mar

REPOSITORIES: biostudies-literature

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Publications

Antibody escape and global spread of SARS-CoV-2 lineage A.27.

Kaleta Tamara T Kern Lisa L Hong Samuel Leandro SL Hölzer Martin M Kochs Georg G Beer Julius J Schnepf Daniel D Schwemmle Martin M Bollen Nena N Kolb Philipp P Huber Magdalena M Ulferts Svenja S Weigang Sebastian S Dudas Gytis G Wittig Alice A Jaki Lena L Padane Abdou A Lagare Adamou A Salou Mounerou M Ozer Egon Anderson EA Nnaemeka Ndodo N Odoom John Kofi JK Rutayisire Robert R Benkahla Alia A Akoua-Koffi Chantal C Ouedraogo Abdoul-Salam AS Simon-Lorière Etienne E Enouf Vincent V Kröger Stefan S Calvignac-Spencer Sébastien S Baele Guy G Panning Marcus M Fuchs Jonas J

Nature communications 20220303 1

In spring 2021, an increasing number of infections was observed caused by the hitherto rarely described SARS-CoV-2 variant A.27 in south-west Germany. From December 2020 to June 2021 this lineage has been detected in 31 countries. Phylogeographic analyses of A.27 sequences obtained from national and international databases reveal a global spread of this lineage through multiple introductions from its inferred origin in Western Africa. Variant A.27 is characterized by a mutational pattern in the ...[more]

PMID: 35241661

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Project description:Since 2020, the receptor-binding domain (RBD) of the spike protein of the novel severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has been constantly mutating, producing most of the notable missense mutations in the context of "variants of concern", probably in response to the vaccine-driven alteration of immune profiles of the human population. The Delta variant, in particular, has become the most prevalent variant of the epidemic, and it is spreading in countries with the highest vaccination rates, causing the world to face the risk of a new wave of the contagion. Understanding the physical mechanism responsible for the mutation-induced changes in the RBD's binding affinity, its transmissibility, and its capacity to escape vaccine-induced immunity is the "urgent challenge" in the development of preventive measures, vaccines, and therapeutic antibodies against the coronavirus disease 2019 (COVID-19) pandemic. In this study, entropy-enthalpy compensation and the Gibbs free energy change were used to analyze the impact of the RBD mutations on the binding affinity of SARS-CoV-2 variants with the receptor angiotensin converting enzyme 2 (ACE2) and existing antibodies. Through the analysis, we found that the existing mutations have already covered almost all possible detrimental mutations that could result in an increase of transmissibility, and that a possible mutation in amino-acid position 498 of the RBD can potentially enhance its binding affinity. A new calculation method for the binding energies of protein-protein complexes is proposed based on the entropy-enthalpy compensation rule. All known structures of RBD-antibody complexes and the RBD-ACE2 complex comply with the entropy-enthalpy compensation rule in providing the driving force behind the spontaneous protein-protein docking. The variant-induced risk of breakthrough infections in vaccinated people is attributed to the L452R mutation's reduction of the binding affinity of many antibodies. Mutations reversing the hydrophobic or hydrophilic performance of residues in the spike RBD potentially cause breakthrough infections of coronaviruses due to the changes in geometric complementarity in the entropy-enthalpy compensations between antibodies and the virus at the binding sites.

Dataset Information

Antibody escape and global spread of SARS-CoV-2 lineage A.27.

Publications

Antibody escape and global spread of SARS-CoV-2 lineage A.27.

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