Page 7 - Binding Affinity News Today

Researchers assessed the different mutations of concern in the SARS-CoV-2 receptor-binding domain.

Researchers assessed the impact of epistatic interactions on the ACE2 affinity in the SARS-CoV-2 Omicron variant.

A team of scientists from China has recently deciphered the structural basis of comparatively higher binding affinity of two Omicron sub-variants, namely B.1.1 and B.2, for human angiotensin-converting enzyme 2 (ACE2).

Researchers generated an AI resource to characterize the T cell epitope landscape for SARS-CoV-2 variants of concern.

A recent study posted to the bioRxiv* preprint server demonstrated various traits, including the entry pathways and sensitivity to vaccination-elicited antibody responses by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron variants.

The study findings showed that the rapid antigen tests with the DMS approach could accurately identify antibody escape mutations in the SARS-CoV-2 N protein.

In a recent study published in the journal Vaccines, researchers revealed how severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) Omicron evades neutralizing antibodies (nAbs).

A recent report published in the STAR Protocols journal depicted a protocol for an antibody-based proximity labeling to discover biotinylated interactors of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2).

In a new study, researchers described their self-designed chimeric receptor-binding domain-dimer vaccine approach to adapt SARS-CoV-2 variants of concern and variants of interest.

The current study, escribes a new mAb LY-CoV1404 (bebtelovimab) from Eli Lilly, with high neutralization potency with a broad spectrum of activity across all current variants.