RBD
receptor-binding domain
SARS-CoV-2 enters cells through the binding of its spike receptor-binding domain (RBD) to the human angiotensin-converting enzyme 2 (ACE2) receptor in concert with accessory receptors/molecules that facilitate viral attachment, internalization, and fusion.
The frequent mutations in the Spike protein, and specifically the receptor binding domain (RBD), resulted in the recommendation by the WHO advisory group to update vaccines with novel antigens.
We measured anti-receptor binding domain (RBD) IgG in milk and maternal and infant blood collected from October to December 2021.
The majority of characteristic mutations in variants of concern (VOCs) have occurred in the NTD and receptor binding domain (RBD).
The aim of this study was to identify factors that lead to a diminished humoral vaccination response in patients with AIRD.MethodsVaccination response was measured with a surrogate virus neutralisation test and by testing for antibodies directed against the receptor-binding-domain (RBD) of SARS-CoV-2 in 308 fully vaccinated patients with AIRD.
AbstractSevere acute respiratory syndrome (SARS) coronaviruses 1 and 2 (SARS-CoV-1 and SARS-CoV-2) derive transmissibility from spike protein activation in the receptor binding domain (RBD) and binding to the host cell angiotensin converting enzyme 2 (ACE2).
However, this pathway results in reduced ability to neutralize S-protein Receptor Binding Domains (RBDs) from several Variants of Concern (VOC) and the rapid waning of memory B cell response requiring vaccine reformulation to cover dominant VOC S-proteins and multiple boosters.
We found Omicron resisted to neutralizing antibody targeting receptor binding domain (RBD) of wildtype SARS-CoV-2.
Newly emerged COVID-19 performs its activity through spike protein receptor binding domain (RBD).
Further, the presence of two loops throughout the SARS-CoV-2 receptor binding domain (RBD) may facilitate binding to the ACE-2 (receptor)throughenhancing the quantity of atoms implicated.
This affinity is given by six amino acid located in the receptor binding domain (RBD) region within the Spike protein.
Immunoglobulin G (IgG) antibodies to receptor-binding domain (RBD) of SARS-CoV-2 spike protein S1 (anti-RBDS1 IgG) was determined in serum by ELISA method.
In this study, we examined the role of the SARS-CoV-2 spike protein receptor-binding domain (RBD) in enhancing VSV-Δ51 viral production and oncolytic activity.
We chose the SARS-CoV-2 receptor binding domain (RBD) as a model system because highly-mutated viral variants have continued to emerge that escape available therapeutics and vaccines.
Here we show that nurse sharks immunized with SARS-CoV-2 recombinant receptor binding domain (RBD), RBD-ferritin (RFN), or spike protein ferritin nanoparticle (SpFN) immunogens elicit a set of new antigen receptor antibody (IgNAR) molecules that target two non-overlapping conserved epitopes on the spike RBD.
Previous studies of SARS-CoV-2 and the closely related SARS-CoV-1 define the receptor binding domain (RBD) portion of the S-protein as the target of most neutralizing antibodies (nAbs).
Despite their divergent evolutionary courses, mutations on their receptor-binding domain (RBD) converge on several hotspots.
SARS-CoV-2 infection depends on the recognition and binding of the cell receptor angiotensin-converting enzyme 2 (ACE2) via the receptor-binding domain (RBD) of the spike protein.
We focused on the detection of neutralization antibody (nAb) in blood circulation to SARS-Cov-2 spike protein receptor binding domain (RBD).
Mutations at positions 452 and 486 of the spike glycoprotein receptor binding domain (RBD) in the SARS-CoV-2 XBC.1 variant were analysed from the viewpoint of change in hydrophobicity and amino acid chargereceptor binding domain (RBD) in the SARS-CoV-2 XBC.1 variant were analysed from the viewpoint of change in hydrophobicity and amino acid charge.