A structure-function analysis shows SARS-CoV-2 BA. 2.86 balances antibody escape and ACE2 affinity
Summary BA. 2.86, a recently described sublineage of SARS-CoV-2 Omicron, contains
many mutations in the spike gene. It appears to have originated from BA. 2 and is distinct …
many mutations in the spike gene. It appears to have originated from BA. 2 and is distinct …
Deep mutational scans for ACE2 binding, RBD expression, and antibody escape in the SARS-CoV-2 Omicron BA. 1 and BA. 2 receptor-binding domains
SARS-CoV-2 continues to acquire mutations in the spike receptor-binding domain (RBD)
that impact ACE2 receptor binding, folding stability, and antibody recognition. Deep …
that impact ACE2 receptor binding, folding stability, and antibody recognition. Deep …
[PDF][PDF] Emergence of SARS-CoV-2 spike RBD mutants that enhance viral infectivity through increased human ACE2 receptor binding affinity
J Ou, Z Zhou, R Dai, S Zhao, X Wu, J Zhang, W Lan… - BioRxiv, 2020 - scholar.archive.org
The current global pandemic of COVID-19 is caused by a novel coronavirus SARS-CoV-2.
The SARS-CoV-2 spike protein receptor-binding domain (RBD) is the critical determinant of …
The SARS-CoV-2 spike protein receptor-binding domain (RBD) is the critical determinant of …
The circulating SARS-CoV-2 spike variant N439K maintains fitness while evading antibody-mediated immunity
SARS-CoV-2 can mutate to evade immunity, with consequences for the efficacy of emerging
vaccines and antibody therapeutics. Herein we demonstrate that the immunodominant …
vaccines and antibody therapeutics. Herein we demonstrate that the immunodominant …
SARS-CoV-2 RBD in vitro evolution follows contagious mutation spread, yet generates an able infection inhibitor
J Zahradník, S Marciano, M Shemesh, E Zoler… - BioRxiv, 2021 - biorxiv.org
SARS-CoV-2 is continually evolving, with more contagious mutations spreading rapidly.
Using in vitro evolution to affinity maturate the receptor-binding domain (RBD) of the spike …
Using in vitro evolution to affinity maturate the receptor-binding domain (RBD) of the spike …
Mutational hotspot in the SARS-CoV-2 Spike protein N-terminal domain conferring immune escape potential
Global efforts are being made to monitor the evolution of SARS-CoV-2, aiming for early
identification of genotypes providing increased infectivity or virulence. However, viral …
identification of genotypes providing increased infectivity or virulence. However, viral …
[HTML][HTML] SARS-CoV-2 spike L452R variant evades cellular immunity and increases infectivity
C Motozono, M Toyoda, J Zahradnik, A Saito… - Cell host & …, 2021 - cell.com
Many SARS-CoV-2 variants with naturally acquired mutations have emerged. These
mutations can affect viral properties such as infectivity and immune resistance. Although the …
mutations can affect viral properties such as infectivity and immune resistance. Although the …
[HTML][HTML] Deep mutational scanning of SARS-CoV-2 receptor binding domain reveals constraints on folding and ACE2 binding
The receptor binding domain (RBD) of the SARS-CoV-2 spike glycoprotein mediates viral
attachment to ACE2 receptor and is a major determinant of host range and a dominant target …
attachment to ACE2 receptor and is a major determinant of host range and a dominant target …
Cross-species tropism and antigenic landscapes of circulating SARS-CoV-2 variants
Y Zhang, M Wei, Y Wu, J Wang, Y Hong, Y Huang… - Cell Reports, 2022 - cell.com
Mutations in the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike
receptor-binding domain (RBD) may alter viral host tropism and affect the activities of …
receptor-binding domain (RBD) may alter viral host tropism and affect the activities of …
Single-virus tracking reveals variant SARS-CoV-2 spike proteins induce ACE2-independent membrane interactions
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) became a global health
crisis after its emergence in 2019. Replication of the virus is initiated by binding of the viral …
crisis after its emergence in 2019. Replication of the virus is initiated by binding of the viral …