Florence Guivel‐Benhassine

This study examines how SARS-CoV-2 RBD antibodies differ in function, showing that neutralizing antibodies lose effectiveness against variants but retain effector functions, while non-neutralizers remain broadly reactive but less effective overall.

This study shows human coronavirus HKU1 replicates more efficiently at nasal temperature (33°C) than at body temperature (37°C), with differences in innate immune response and viral stability.

The paper identifies DNA-PKcs as a regulator of cyclic dinucleotide signaling, showing it interacts with CDN and modulates STING activation and antiviral responses.

This study shows TMPRSS2 reduces antibody binding to SARS-CoV-2 spike by altering its structure and shedding, but not virion infectivity.

This study shows that the SARS-CoV-2 Omicron variant replicates more efficiently and evades innate immune responses in a nasal epithelium model at physiological temperature.

The paper identifies OPG153 as a target of broadly neutralizing antibodies against MPXV and related viruses using antigen-agnostic isolation, AlphaFold 3 modeling, and cryo-EM.

The paper develops a pipeline to generate potent Affitins targeting SARS-CoV-2 spike protein RBD, achieving high neutralization potency with IC50 values as low as 0.8 pM.

The paper identifies and characterizes monoclonal antibodies targeting the Mpox A28 protein, showing potent neutralization of Mpox and Vaccinia virus through complement-dependent mechanisms and providing protection in mice.

This study evaluates Tecovirimat's antiviral activity against four Mpox virus clades and finds it effectively inhibits all at nanomolar concentrations.

This study shows that SARS-CoV-2 entry and fusion depend on cholesterol but not on ACE2 localization to lipid rafts.

The paper evaluates the neutralization activity of two new monoclonal antibodies against emerging SARS-CoV-2 variants and finds reduced efficacy against some sublineages.