literature

SARS_CoV_2 mutation literature information.

Engineered small extracellular vesicles displaying ACE2 variants on the surface protect against SARS-CoV-2 infection.

PMID: 34982509 2022 Journal of extracellular vesicles

Result: We assessed the neutralization efficacy of engineered sEVs expressing sACE2.v1 with H34A, T92Q, Q325P, and A386L, as well as sACE2.v2 containing T27Y, L79T, N330Y, and A386L.

Fast Prediction of Binding Affinities of the SARS-CoV-2 Spike Protein Mutant N501Y (UK Variant) with ACE2 and Miniprotein Drug Candidates.

PMID: 33881861 2021 The journal of physical chemistry. B

Introduction: To investigate the potential change in binding affinity associated with the N501Y mutation, we have modeled both the SARS-CoV-2 spike protein and its N501Y mutant binding with wild-type human ACE2 (hACE2) and a previously reported T27Y/L79T/N330Y mutant of ACE2 (known as ACE2.v2.4) which has a 40-fold increased binding affinity with the wild-type spike protein of SARS-CoV-2.

Method: In brief, using the cryo-EM structure (RCSB: 7KMB) of the spike/ACE2 complex, after the energy-minimization, the reported mutant of the spike mutant (N501Y) or ACE2 mutant (ACE2v2 and ACE2.v2.4) in the spike/ACE2 complex was reconstructed using the PyMol m

S19W, T27W, and N330Y mutations in ACE2 enhance SARS-CoV-2 S-RBD binding toward both wild-type and antibody-resistant viruses and its molecular basis.

PMID: 34531369 2021 Signal transduction and targeted therapy

Abstract: Here we show that mutations of S19W, T27W, and N330Y in ACE2 could individually enhance SARS-CoV-2 S-RBD binding.

Abstract: Taken together, our biochemical and structural data have delineated the basis for the elevated S-RBD binding associated with S19W, T27W, and N330Y mutations in ACE2, paving the way for potential application of these mutants in clinical treatment of COVID-19.

Machine learning guided design of high affinity ACE2 decoys for SARS-CoV-2 neutralization.

PMID: 34981064 2021 bioRxiv

Introduction: Double mutants containing the combination of sACE22.v2.4 mutations, T27Y;L79T, T27Y;N330Y, and L79T;N330Y, bound to RBD with greater affinity than the single mutant variants, and had similar affinity as sACE22.v2.4.

Introduction: For the L91P;N330Y mutant, both single mutations exhibited a relative binding fold enhancement of under two; however, when expressed together, the relative binding increased over 2.5 fold.

Introduction: They further characterized a sACE2 derivative containing the three mutations T27Y, L79T, and N330Y, referred to as sACE22.v2.4 (Figure 1A), to exhibit a 35-fold increase in binding affinity to SARS-CoV-2, and further tighter affinity

An engineered decoy receptor for SARS-CoV-2 broadly binds protein S sequence variants.

PMID: 33398275 2020 bioRxiv

Result: N501 of S is located in the 498-506 loop and its substitution to large aromatic side chains might alter the loop conformation to cause steric strain with nearby ACE2 mutation N330Y in sACE22.v2.4.

Result: Soluble ACE22.v2.4 has three mutations from wild type ACE2: T27Y buried within the RBD interface, and L79T and N330Y at the interface periphery (Figure 5A).

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