literature

SARS_CoV_2 mutation literature information.

Structural Modeling of the SARS-CoV-2 Spike/Human ACE2 Complex Interface can Identify High-Affinity Variants Associated with Increased Transmissibility.

PMID: 33992693 2021 Journal of molecular biology

Result: Averaged affinities predicted by structural modeling indicate that the mutations fall into three groups (Figure 6 (a)): very high-affinity (80 to 90% better that WT; S477N/E484K/N501Y, S477N/E484K and E484K/N501Y), high-affinity (40 to 50% better than WT; S477N, E484K, N501Y), WT-like (S477N/N501Y, K417T/E484K/N501Y, N439K, Y453F), and low-affinity (<70% of WT; K417T<

A SARS-CoV-2 vaccine candidate would likely match all currently circulating variants.

PMID: 32868447 2020 Proc Natl Acad Sci U S A

Result: The others were nonsynonymous: G476S (n = 10 sequences, 0.05%), Y453F (n = 5, 0.02%), G446V (n = 3, 0.02%), and A475V (n = 2, 0.01%).

Neutralising antibodies in Spike mediated SARS-CoV-2 adaptation.

PMID: 33398302 2020 medRxiv

Introduction: There it was associated with the RBD mutation Y453F in almost 200 individuals.

Mutational spectra of SARS-CoV-2 isolated from animals.

PMID: 33384909 2020 PeerJ

Abstract: SARS-CoV-2 isolates from minks exhibited two amino acid substitutions (G261D, A262S) in the N-terminal domain of S protein and four (L452M, Y453F, F486L, N501T) in the receptor-binding motif (RBM).

Result: Fifteen unique mutations were identified in mink isolates (Table S2), four of which (L452M, Y453F, F486L, N501T) were located within the RBM of S protein.

Discussion: Similarly, Y453F involved tyrosine and phenylalanine, and both are hydrophobic and aromatic.

Browser Board

Co-occurred Entities

Filtrator