ArticleAllergy2022
In vitro data suggest that Indian delta variant B.1.617 of SARS-CoV-2 escapes neutralization by both receptor affinity and immune evasion.
Article in Allergy, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers, 1 of them a synthesis that pooled it.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
45 citing papers in PubMed, 1 synthesis or guideline pooled it, 89 citations in OpenAlex.
- Reinfection in patients with COVID-19: a systematic review.Global health research and policy · 2022Pooled it
- Impact of SARS-CoV-2 RBM Mutations N501Y and E484K on ACE2 Binding: A Combined Computational and Experimental Study.International journal of molecular sciences · 2025Article
- Tracking down the origin and subsequent spread of SARS-CoV-2 lineage B.1.619.Virus evolution · 2025Article
- Vaccination status and disease severity of COVID-19 in different phases of the pandemic.Human vaccines & immunotherapeutics · 2024Article
- Binding affinity between coronavirus spike protein and human ACE2 receptor.Computational and structural biotechnology journal · 2024Review
- Disease severity of COVID-19 in different phases of the pandemic: Do healthcare workers have better outcomes?Vaccine: X · 2023Article
- Facile electrochemical affinity measurements of small and large molecules.RSC advances · 2023Article
- Intrinsic D614G and P681R/H mutations in SARS-CoV-2 VoCs Alpha, Delta, Omicron and viruses with D614G plus key signature mutations in spike protein alters fusogenicity and infectivity.Medical microbiology and immunology · 2023Article
- SARS-CoV-2 replication in airway epithelia requires motile cilia and microvillar reprogramming.Cell · 2023Article
- Vaccination using mutated receptor binding domains of SARS-CoV-2: Evidence for partial immune escape but not serotype formation.Frontiers in immunology · 2023Article
- Taking stock of the mutations in human SARS-CoV-2 spike proteins: From early days to nearly the end of COVID-19 pandemic.Current research in structural biology · 2023Article
- Evaluation of an identification method for the SARS-CoV-2 Delta variant based on the amplification-refractory mutation system.Frontiers in cellular and infection microbiology · 2023Article
- A two-ward acute care hospital outbreak of SARS-CoV-2 delta variant including a point-source outbreak associated with the use of a mobile vital signs cart and sub-optimal doffing of personal protective equipment.The Journal of hospital infection · 2023Article
- Reduction in COVID-19 Vaccine Effectiveness against SARS-CoV-2 Variants in Seoul according to Age, Sex, and Symptoms: A Test-Negative Case-Control Study.International journal of environmental research and public health · 2022Article
- Article
- Strain wars 3: Differences in infectivity and pathogenicity between Delta and Omicron strains of SARS-CoV-2 can be explained by thermodynamic and kinetic parameters of binding and growth.Microbial risk analysis · 2022Article
- Strain wars 5: Gibbs energies of binding of BA.1 through BA.4 variants of SARS-CoV-2.Microbial risk analysis · 2022Article
- Novel coronavirus mutations: Vaccine development and challenges.Microbial pathogenesis · 2022Review
- Identification of hACE2-interacting sites in SARS-CoV-2 spike receptor binding domain for antiviral drugs screening.Virus research · 2022Article
- Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 3 countries.
Funding
Abstract
backgroundEmerged mutations can be attributed to increased transmissibility of the B.1.617 and B.1.36 Indian delta variants of SARS-CoV-2, most notably substitutions L452R/E484Q and N440K, respectively, which occur in the receptor-binding domain (RBD) of the Spike (S) fusion glycoprotein.
objectiveWe aimed to assess the effects of mutations L452R/E484Q and N440K (as well as the previously studied mutation E484K present in variants B.1.351 and P.1) on the affinity of RBD for ACE2, SARS-CoV-2 main receptor. We also aimed to assess the ability of antibodies induced by natural infection or by immunization with BNT162b2 mRNA vaccine to recognize the mutated versions of the RBD, as well as blocking the interaction RBD-ACE2, an important surrogate readout for virus neutralization.
methodsTo this end, we produced recombinant wild-type RBD, as well as RBD containing each of the mutations L452R/E484Q, N440K, or E484K (the latest present in variants of concern B.1.351 and P.1), as well as the ectodomain of ACE2. Using Biolayer Interferometry (BLI), we measured the binding affinity of RBD for ACE2 and the ability of sera from COVID-19 convalescent donors or subjects immunized with BNT162b2 mRNA vaccine to block this interaction. Finally, we correlated these results with total anti-RBD IgG titers measured from the same sera by direct ELISA.
resultsThe binding assays showed L452R/E484Q double-mutant RBD to interact with ACE2 with higher affinity (K
conclusionOur data suggest that the newly emerged SARS-CoV-2 variant B.1.617, as well as the better-studied variants B.1.351 and P.1 (all containing a mutation at position E484) display increased transmissibility both due to their higher affinity for the cell receptor ACE2 and their ability to partially bypass immunity generated against the wild-type virus. For variant B.1.36 (with a point mutation at position N440), only increased affinity seems to play a role.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.