ArticleJournal of medical virology2021
SARS-CoV-2 B.1.617 Indian variants: Are electrostatic potential changes responsible for a higher transmission rate?
Article in Journal of medical virology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.
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Who cites it
69 citing papers in PubMed.
- Structural Analysis of the SARS-CoV-2 Spike N-Terminal Domain Across Wild-Type and Recent Variants: A Comparative Study.Proteins · 2025Article
- Outbreak dates of virus could be predicted by their protein sequence.Journal of translational medicine · 2025Article
- Effect of mild-to-moderate COVID‑19 on the incidence and risk factors for deep vein thrombosis in patients with hip fracture: a retrospective study.BMC surgery · 2025Article
- Impact of Vaccination on Intra-Host Genetic Diversity of Patients Infected with SARS-CoV-2 Gamma Lineage.Viruses · 2024Article
- COVID-19 mutations: An overview.World journal of methodology · 2024Review
- Article
- Genome sequencing of severe acute respiratory syndrome COVID-19 EF.1 variant strain obtained from a Moroccan patient.Microbiology resource announcements · 2024Article
- On the SARS-CoV-2 Variants.Infectious disease reports · 2024Article
- Three-Dimensional Structural Stability and Local Electrostatic Potential at Point Mutations in Spike Protein of SARS-CoV-2 Coronavirus.International journal of molecular sciences · 2024Article
- A study on the effect of natural products against the transmission of B.1.1.529 Omicron.Virology journal · 2023Review
- Omicron Coronavirus: pH-Dependent Electrostatic Potential and Energy of Association of Spike Protein to ACE2 Receptor.Viruses · 2023Article
- A tale of two waves: Delineating diverse genomic and transmission landscapes driving the COVID-19 pandemic in Pune, India.Journal of infection and public health · 2023Article
- Peculiar Variations of the Electrostatic Potential of Spike Protein N-terminal Domain Associated with the Emergence of Successive SARS-CoV-2 Omicron Lineages.The Journal of infection · 2023Article
- Zoonosis and zooanthroponosis of emerging respiratory viruses.Frontiers in cellular and infection microbiology · 2023Review
- Single-virus tracking reveals variant SARS-CoV-2 spike proteins induce ACE2-independent membrane interactions.Science advances · 2022Article
- Delta variant (B.1.617.2) of SARS-CoV-2: Mutations, impact, challenges and possible solutions.Human vaccines & immunotherapeutics · 2022Review
- Targeting an evolutionarily conserved "E-L-L" motif in spike protein to identify a small molecule fusion inhibitor against SARS-CoV-2.PNAS nexus · 2022Article
- Differential avidity determination of IgG directed towards the receptor-binding domain (RBD) of SARS-CoV-2 wild-type and its variants in one assay: Rational tool for the assessment of protective immunity.Journal of medical virology · 2022Article
- Omicron (B.1.1.529) - A new heavily mutated variant: Mapped location and probable properties of its mutations with an emphasis on S-glycoprotein.International journal of biological macromolecules · 2022Article
- Omicron variant (B.1.1.529) and its sublineages: What do we know so far amid the emergence of recombinant variants of SARS-CoV-2?Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2022Review
9 more citing papers are in PubMed but not listed here.
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12 authors.
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Abstract
Lineage B.1.617+, also known as G/452R.V3 and now denoted by WHO with the Greek letters δ and κ, is a recently described SARS-CoV-2 variant under investigation first identified in October 2020 in India. As of May 2021, three sublineages labeled as B.1.617.1 (κ), B.1.617.2 (δ), and B.1.617.3 have been already identified, and their potential impact on the current pandemic is being studied. This variant has 13 amino acid changes, three in its spike protein, which are currently of particular concern: E484Q, L452R, and P681R. Here, we report a major effect of the mutations characterizing this lineage, represented by a marked alteration of the surface electrostatic potential (EP) of the receptor-binding domain (RBD) of the spike protein. Enhanced RBD-EP is particularly noticeable in the B.1.617.2 (δ) sublineage, which shows multiple replacements of neutral or negatively charged amino acids with positively charged amino acids. We here hypothesize that this EP change can favor the interaction between the B.1.617+ RBD and the negatively charged ACE2, thus conferring a potential increase in the virus transmission.
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