Mélanie Ott

The paper tracks SARS-CoV-2 mutations over 90 days in an HIV-positive individual and tests their functional impact on viral entry and replication.

This study shows that SARS-CoV-2's ORF8 protein reprograms macrophages to enhance viral infection of lung epithelial cells, contributing to lung pathology in COVID-19.

This paper introduces LUCas, a light-controlled Cas13a system that suppresses background activity and enables precise control of RNA detection, improving assay sensitivity and enabling multiplexed viral co-infection detection.

The paper develops a bead-based Cas13a assay called SurfCas for sensitive and multiplexed RNA detection, showing it matches bulk reaction sensitivity and works in complex biological samples.

The paper investigates how mutations in SARS-CoV-2 M and N proteins balance viral particle assembly and immune evasion through co-evolution.

This study identifies multiple dispersed packaging signals in the SARS-CoV-2 genome that cooperate to direct RNA packaging into virions, revealing a dynamic mechanism for coronavirus genome assembly.

The paper links protease sequence variation to biochemical parameters and viral fitness using high-throughput enzymology and replication assays.

This paper identifies AVI-6451, an orally bioavailable inhibitor of SARS-CoV-2 Mac1 with once-daily efficacy in a mouse model.

This study identifies the non-spike R204P mutation in the SARS-CoV-2 Omicron XEC variant as a driver of increased inflammation and pathogenicity through NF-κB activation.

The paper identifies phospholipidosis as a common artifact in antiviral drug repurposing and introduces a microplate-based assay to detect it, finding that 65% of tested drugs induce it.

This study identifies Mac1 as a therapeutic target for SARS-CoV-2 and demonstrates that AVI-4206, a small molecule inhibitor, reduces viral replication and improves survival in an animal model.

This paper develops RocASO, a molecular glue-oligonucleotide conjugate that selectively inhibits mRNA translation by targeting specific sequences, showing potent antiviral activity against SARS-CoV-2.

This paper describes the discovery of new coronavirus MPro inhibitors with improved pharmacokinetics, broad-spectrum antiviral activity, and superior in vivo efficacy compared to existing drugs.

This study identifies the L260F mutation in NSP6 as enhancing RNA replication and pathogenesis in recent SARS-CoV-2 variants, independent of Spike function.

The paper resolves the x-ray structure of SARS-CoV and SARS-CoV-2 SUD-N/M domains and shows they have rotational flexibility, with disulfide bonds absent in pangolin-SARS and related viruses.

This study shows ORF8 suppresses viral particle production by interacting with Spike and causing Golgi fragmentation, supporting evolutionary pressure to delete ORF8 in SARS-CoV-2 variants.

This study demonstrates that de novo-designed minibinders can be adapted to various cell engineering tools, improving antigen detection and cytotoxicity compared to antibody-based systems.

This paper develops covalent nanobodies using a PERx mechanism to neutralize SARS-CoV-2 and variants with greatly increased potency.

The paper shows that BET proteins are antiviral factors against SARS-CoV-2, and the viral E protein neutralizes BET-mediated post-entry antiviral effects.

A computational drug repositioning pipeline identifies potential therapeutics for COVID-19 by matching SARS-CoV-2 gene expression signatures to drug profiles.

This paper introduces SARSNotch, a sentinel cell system that detects SARS-CoV-2 Spike protein and triggers genetic responses in cell lines and T lymphocytes.

In primary human cortical tissue and stem cell-derived organoids, SARS-CoV-2 infects astrocytes almost exclusively, apparently through DPP4 rather than ACE2, leaving them reactive and stressed.

Affinity-purification mass spectrometry of 26 SARS-CoV-2 proteins in HEK293T cells yields 332 high-confidence host interactions and 67 druggable human proteins with known compounds.

The paper investigates how acetylation and phosphorylation of RNA polymerase II CTD interact through RPRD proteins, showing acetylation regulates phosphorylation and vice versa.