Key result
VH3-53/3-66-derived public neutralizing antibodies, particularly BD-218 and BD-604, maintained high binding affinity and neutralizing efficacy against most naturally occurring SARS-CoV-2 RBD variants.
Why the study?
Whether SARS-CoV-2 receptor binding domain mutations alter virus-host cell interactions and gain resistance to neutralizing antibodies needed to be addressed.
Do VH3-53/3-66 class-derived public antibodies maintain neutralization efficacy against naturally occurring SARS-CoV-2 RBD variants?
Do VH3-53/3-66 class-derived public antibodies maintain neutralization efficacy against naturally occurring SARS-CoV-2 RBD variants?
Structural analyses reveal that while some SARS-CoV-2 RBD mutations escape specific neutralizing antibodies, the prevalent VH3-53/3-66 class-derived public antibodies largely retain their efficacy against most variants.
Answers are grounded in this paper and cite their sources.
May support mAb therapeutic design against variants; leaves open clinical validation in evolving SARS-CoV-2.
SARS-CoV-2 variants are developing rapidly among COVID-19 patients, likely resulting in higher transmissibility at the population level. 1 , 2 , 3 , 4 , 5 Mutations in the spike proteins (S proteins) of these variants are supposed to be related with receptor binding and virus invasion. Examples of these prevalent variants include the B.1.1.7 lineage that emerged in the United Kingdom (UK), the B.1.351 lineage (also termed 501Y.V2) in South Africa (SA), and the P.1 and P.2 lineages in Brazil, etc. Many S protein alterations, especially in the receptor binding domain (RBD), characterize these variants, e.g., the N501Y mutation in B.1.351 and the K417N (or T)/E484K/N501Y co-mutation in the SA and Brazil variant. 2 , 3 , 5 The RBD is responsible for interacting with mammalian receptor angiotensin-converting enzyme 2 (ACE2) to mediate the viral infection of host cells. It is also concentrated with epitopes for neutralizing antibodies (NAbs), thus playing a vital role in the study of prophylactics and therapeutics for COVID-19. 6 , 7 , 8 , 9 , 10 Whether those RBD mutations may alter virus–host cell interactions and gain resistance to NAbs needs to be addressed.
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Xu et al. (2021) conducted a letter in SARS-CoV-2. Neutralizing antibodies (e.g., BD-218, BD-604) vs. SARS-CoV-2 wild-type and variants was evaluated on Binding affinity and neutralization efficacy against SARS-CoV-2 RBD variants. VH3-53/3-66-derived public neutralizing antibodies, particularly BD-218 and BD-604, maintained high binding affinity and neutralizing efficacy against most naturally occurring SARS-CoV-2 RBD variants.
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