Researchers from The University of Texas MD Anderson Cancer Center have developed fully human bispecific antibodies, as revealed in a recent study. These antibodies can bind to two distinct epitopes of the receptor binding domain (RBD) of the SARS-CoV-2 spike protein and have demonstrated the ability to neutralize various strains of the virus, including the Omicron variant.
In a recent study posted to the medRxiv preprint server, researchers in France explored the relationship between long-term immunoglobulin (Ig)-A response to severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and taste and smell disorders.
A recent Nature Reviews Immunology study has summarized the efficacy of neutralizing antibodies that target four main regions of the spike (S) protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), namely, the receptor-binding domain (RBD) in the S1 subunit, the fusion peptide region in the S2 subunit, the stem helix region, and the N-terminal domain.
In a recent study published in the Journal of Medical Virology, Italian researchers investigated the presence of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) ribonucleic acid (RNA) and antibodies (Abs) in the milk of breastfeeding mothers with SARS-CoV-2 infections.
A recent article posted to the bioRxiv preprint server demonstrated structural underpinnings of the neutralization of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron variants by 002-S21F2, an extensive SARS-CoV-2 neutralizing antibody.