literature

SARS_CoV_2 mutation literature information.

Molecular Analysis of SARS-CoV-2 Genetic Lineages in Jordan: Tracking the Introduction and Spread of COVID-19 UK Variant of Concern at a Country Level.

PMID: 33807556 2021 Pathogens (Basel, Switzerland)

Introduction: the UK variant of concern) that was detected in the UK in September 2020 with N501Y and P681H as the most notable amino acid substitutions; (5) lineage B.1.351 which dates back to December 2020 (the South African variant) with N501Y, K417N, and E484K as the most notable amino acid substitutions; and (6) lineage P.1 (the Brazilian variant) that was first detected in December 2020 with N501Y, and E484K as the most notable amino acid substitutions.

Method: The measur

Result: The following amino acid substitutions were totally absent from the sequences that were analyzed in this study: K417N and E484K.

Ultrapotent bispecific antibodies neutralize emerging SARS-CoV-2 variants.

PMID: 33821267 2021 bioRxiv

Method: B.1.351 virus contained the following spike mutations: L18F, D80A, D215G, del-L242_244, R246I, K417N, E484K, N501Y, D614G, A701V.

Table: K417N

Complete map of SARS-CoV-2 RBD mutations that escape the monoclonal antibody LY-CoV555 and its cocktail with LY-CoV016.

PMID: 33842902 2021 Cell reports. Medicine

Result: Of particular note, the B.1.351 (also known as 20H/501Y.V2) and P.1 (also known as 20J/501Y.V3) lineages contain combinations of mutations (E484K and K417N/T) that individually escape each antibody (Figure 2B), suggesting that the LY-CoV555+LY-CoV016 cocktail may be ineffective against these lineages.

Result: The escape mutations present at the highest frequency among the sequenced isolates are E484K, L452R, and S494P for LY-CoV555 and K417N/T for LY-C

Result: have reported that E484K and K417N dramatically and specifically reduce neutralization by LY-CoV555 and LY-CoV016, respectively, while N501Y has no impact on neutralization by either antibody.

Antibody evasion by the P.1 strain of SARS-CoV-2.

PMID: 33852911 2021 Cell

Figure: (E and F) K417N/T interactions with Fab 222 (E) and N501Y interactions with Fab 222 (F) in the K417N (cyan), K417T (magenta), P.1 (blue), and P.1.351 (teal) RBD-Fab 222 complex structures compared with the WT RBD-Fab 222 (gray) complex by superimposing the Discussion: Comparison of neutralization of pseudoviruses expressing only the three RBD mutations (K417N, E484K, and N501Y) of B.1.351 with pseudovirus expressing the full suite of mutations in B.1.351 spike shows that the non-RBD changes substantially increase escape from neutralization.

Vaccine Breakthrough Infections with SARS-CoV-2 Variants.

PMID: 33882219 2021 The New England journal of medicine

Discussion: In January 2021, Moderna announced clinical efforts to target a new variant of SARS-CoV-2 that was first identified in South Africa and includes three mutations (E484K, N501Y, and K417N) in the angiotensin-converting-enzyme 2 receptor-binding domain.

Nanobody cocktails potently neutralize SARS-CoV-2 D614G N501Y variant and protect mice.

PMID: 33893175 2021 Proc Natl Acad Sci U S A

Introduction: Within the RBD, B.1.1.7 carries N501Y mutation; B.1.351 carries K417N, E484K, and N501Y mutations; and B.1.1.248 carries K417N/T, E484K, and Discussion: The K417N/T variants would disallow the formation of a salt bridge.

Discussion: Within the RBD, B.1.1.7 harbors the N501Y mutation, whereas B.1.351 has K417N, E484K, and N501Y, and B.1.1.248 has K417T, E484K, and N501Y.

The Genetic Variant of SARS-CoV-2: would It Matter for Controlling the Devastating Pandemic?

PMID: 33907511 2021 International journal of biological sciences

Introduction: The 501Y.V2 variant is characterized by carrying nine mutations in S protein (L18F, D80A, D215G, R246I, Delta242-244, K417N, E484K, N501Y, A701V) (Table 1), three of which (K417N, E484K and N501Y) locate in the RBD of the S protein.

Introduction: The results showed that the neutralization activities of plasma from vaccinated individual to the pseudoviruses expressing N501Y, E484K or K417N

Impact of meteorological parameters and population density on variants of SARS-CoV-2 and outcome of COVID-19 pandemic in Japan.

PMID: 33908339 2021 Epidemiology and infection

Abstract: Cluster mutations namely N501Y (45%), E484K (30%), N439K (16%), K417N (6%) and T478I (3%) at spike protein have increased during January to February 2021.

Result: However, during the second wave starting from October 2020 substitution point mutations E780Q, K417N, T478I,

Discussion: Variants with substitutions namely, K417N, T478I, N501Y, E484K, N439K and S477N at RBDs have been detected recently in Japan.

Impact of the N501Y substitution of SARS-CoV-2 Spike on neutralizing monoclonal antibodies targeting diverse epitopes.

PMID: 33910569 2021 Virology journal

Introduction: In addition, N501Y was also shared by another SARS-CoV-2 variant-N501Y

Method: In addition, the K417N and E484K contribute more than a single N501Y substitution in the resistance of virus to the neutralization by nAbs in a study which measured the neutralizing potencies of eight human nAbs against two SARS-CoV-2 variants both carrying N501Y mutation (N501Y.V1 and N501Y.V2).

Method: Sequence analysis revealed that another two amino acid substitutions (K417N and Q493H) appeared in RBD of SARS-CoV-2 spike besides N501Y.

The Impact on Infectivity and Neutralization Efficiency of SARS-CoV-2 Lineage B.1.351 Pseudovirus.

PMID: 33917138 2021 Viruses

Abstract: Interestingly, K417N and E484K mutations dramatically enhanced cell-cell fusion than N501Y even though their infectivity were similar,

Introduction: Remarkably, B.1.351 contains additional two mutations, K417N and E484K, in receptor binding motif (RBM) of the RBD region and those may potentially induce a conformational change of the spike protein, and subsequently increase the infectivity of B.1.351 than other lineages.

Introduction: We show that SARS-CoV-2 B.1.351 variant harboring K417N and E484K mutations have naturally evolved to possess notable alterations in their infectivity and S1/S2 cleavage, leading to enhanced syncytium formation and antigenicity.

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