literature

The basis of mink susceptibility to SARS-CoV-2 infection.

PMID: 35396646 2022 Journal of applied genetics

Introduction: However, there is no data available that any of the mutations, which were expected to be crucial for SARS-CoV-2 infection in minks (Y453F, F486L, N501T, and D614G), alter S protein glycosylation.

Introduction: In the case of F486L substitution, the coronavirus interrelates L79, M82, Y83, and H79, T82, Y83 residues of human and mink ACE2, respectively.

Introduction: has described that three substitutions (Y453F, F486L, and N501T) facilitate SARS-CoV-2 interaction with different residues of human and mink ACE2, which suggest that having one of these mutations will allow SARS-CoV-2 to infect both human and mink.

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 R408I, L455Y, F486L, Q493N, Q498Y, N501T and the mutations A930V,

PMID: 34915409 2022 International immunopharmacology

Table: F486L

But Mouse, You Are Not Alone: On Some Severe Acute Respiratory Syndrome Coronavirus 2 Variants Infecting Mice.

PMID: 35022734 2022 ILAR journal

Abstract: This effect could be enhanced by mutations in positions 417, 484, and 493 (especially K417N, E484K, Q493K, and Q493R), and to a lesser extent by mutations in positions 486 and 499 (such as F486L and P499T).

Mutations that adapt SARS-CoV-2 to mink or ferret do not increase fitness in the human airway.

PMID: 35093235 2022 Cell reports

Abstract: Here we investigate the molecular basis of mink and ferret adaptation and demonstrate the spike mutations Y453F, F486L, and N501T all specifically adapt SARS-CoV-2 to use mustelid ACE2.

Result: For example, Spike-Y453F lies close to ACE2-34 (histidine in human ACE2, tyrosine in mustelid), Spike-N501T lies close to ACE2-354, and Spike-F486L lies between ACE2 residues 79, 82, and 24 (Figure 3D).

Result: Interestingly, by investigating all SARS-CoV-2 sequences isolated from mink reported on the Global Initiative on Sharing All Influenza Data (GISAID), we and others noted that N501T,

PMID: 35266951 2022 Genetics and molecular biology

Introduction: Regarding SARS-CoV-2, the coronavirus RaTG13 of the brown bat (Rhinolophs affinis) is a potential ancestor.Their genomes have 97.41% identity ; however, at least five amino acid (aa) substitutions (F486L, Q493Y, S494R, N501D, and Y505H) at critical sites of the Spike (S) glycoprotein receptor-binding domain (RBD) of RaTG13 are crucial for the Wuhan-SARS-CoV-2 lineage to acquire high tropism with its cognate human cell receptor (cell-surface peptidase angiotensin-converting enzyme 2, ACE2).

Introduction: The first strain of SARS-CoV-2 identified in Wuhan, China, in December 2019, was also characterized as having five critical amino acid differences in its RBD when

Allosteric Determinants of the SARS-CoV-2 Spike Protein Binding with Nanobodies: Examining Mechanisms of Mutational Escape and Sensitivity of the Omicron Variant.

PMID: 35216287 2022 International journal of molecular sciences

Introduction: These studies identified a group of common resistant mutations in the dynamic RBM region (F490S, E484K, Q493K/R, F490L, F486S, F486L, and Y508H) that evade many individual nanobodies.

Result: The mutational sensitivity map also sheds some light on the structure-functional role of sites targeted by common resistant mutations (F490S, E484K, Q493K/R, F490L, F486S, F486L, and Y508H) that evade many individual nanobodies.

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

Result: To examine the dynamic behavior, MD simulation runs for 10 ns to contemplate the structural stability of RBD mutant variants (F486L, Q493N, B.1.617, R408I, L455Y, K417G and E484K) in comparison to wild type.

Result: We found that seven mutant variants (F486L, Q493N, B.1.617 (L452R & E484Q), R408I, L455Y, K417G and E484K) have structural changes in RBD region (S3).

Result: We found that seven structurally changed

Review of the mechanisms of SARS-CoV-2 evolution and transmission.

PMID: 34545334 2021 ArXiv

Introduction: A list of vaccine-escape (vaccine-breakthrough) mutations was tabulated in our early work, including S494P, Q493L, K417N, F490S, F486L, R403K, E484K, L452R, K417T, F490L, E484Q, and A475S.

Introduction: Many of these co-mutation sets involve vaccine-escape mutations predicted in our early work: S494P, Q493L, K417N, F490S, F486L, R403K,

PMID: 34642638 2021 ArXiv

Introduction: Later on, we have provided a list of most likely vaccine escape RBD mutations with high frequency, including S494P, Q493L, K417N, F490S, F486L, R403K, E484K, L452R, K417T, F490L, E484Q, and A475S.