literature

SARS_CoV_2 mutation literature information.

Insights into the structural and dynamical changes of spike glycoprotein mutations associated with SARS-CoV-2 host receptor binding.

PMID: 32851910 2022 Journal of biomolecular structure & dynamics

Abstract: In our study, several mutations like R408I, L455Y, F486L, Q493N, Q498Y, N501T of RBD (319-591), and A930V, D936Y of HR1 (912-984) have been studied to examine its role on the spike glycoprotein native structure.

Introduction: The important RBD mutations like

Introduction: reported various mutations on spike glycoprotein and also highlighted the importance of R408I mutation responsible for lower ACE2 binding which revealed a higher risk of COVID-19 pandemic (Jia et al.,).

Impact of B.1.617 and RBD SARS-CoV-2 variants on vaccine efficacy: An in-silico approach.

PMID: 35370005 2022 Indian journal of medical microbiology

Discussion: A few mutants' viz.L455Y, Q493N, R408I, Q498Y, F486L, N501T within the RBD region (319-591), and D936Y& A930V within HR1 site (912-984) have also been studied by in silico analysis to investigate the basic structure of spike glycoprotein.

Discussion: Comparison of wild with mutant RBD protein, significant RMSD fluctuations were observed in all variants (B.1.617 0.25-0.5 nm, E484K nm 0.25-0.4 nm, F486L 0.2-0.3 nm, K417G 0.2-0.4 nm, L455Y 0.2-0.4 nm,

Computational investigation reveals that the mutant strains of SARS-CoV2 have differential structural and binding properties.

PMID: 34968787 2022 Computer methods and programs in biomedicine

Introduction: R408I (Arginine 408 to Isoleucine) mutant isolated from India.

Introduction: The rest of mutations V367F and R408I, mostly affected the overall topology and stability of RBD as these mutations present at the loop regions of N-terminal and turn that connect beta-sheet3 and 4, respectively.

Introduction: These mutations (V367F, R408I

E484K and N501Y SARS-CoV 2 spike mutants Increase ACE2 recognition but reduce affinity for neutralizing antibody.

PMID: 34915409 2022 International immunopharmacology

Table: R408I

Functional and Structural Characterization of SARS-Cov-2 Spike Protein: An In Silico Study.

PMID: 34158771 2021 Ethiopian journal of health sciences

Table: R408I

Characterization of SARS-CoV-2 different variants and related morbidity and mortality: a systematic review.

PMID: 34103090 2021 European journal of medical research

Table: R408I

Bioinformatics Analysis Unveils Certain Mutations Implicated in Spike Structure Damage and Ligand-Binding Site of Severe Acute Respiratory Syndrome Coronavirus 2.

PMID: 34121839 2021 Bioinformatics and biology insights

Result: Eighty four whole spike protein sequences isolated from Africa are used, and the most common mutations are found to be Q667H (5 mutations), D614G (3 mutations), R408I (2 mutations), and others (1 mutations), which was found containing 8 different mutations (Table 1).

Table: R408I

Epitope Classification and RBD Binding Properties of Neutralizing Antibodies Against SARS-CoV-2 Variants of Concern.

PMID: 34149735 2021 Frontiers in immunology

Result: Finally, there are several common contact residues in the C4 NAb epitope, suggesting that N370S, T376I, V382L, P384L, T385I, and R408I could disrupt C4 NAbs.

Characterization of SARS-CoV-2 worldwide transmission based on evolutionary dynamics and specific viral mutations in the spike protein.

PMID: 34419160 2021 Infectious diseases of poverty

Table: R408I

A bioluminescent and homogeneous SARS-CoV-2 spike RBD and hACE2 interaction assay for antiviral screening and monitoring patient neutralizing antibody levels.

PMID: 34531417 2021 Scientific reports

Method: The following proteins were purchased from Sino Biological (Beijing, China): SARS-CoV-2 recombinant Spike RBD wild type, RBD (S477N), RBD (Y453F), RBD (K458R), RBD (F342L), RBD (V367F), RBD (N354D), RBD (A435S), RBD (V483A), RBD (W436R), RBD

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