Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural basis for varying drug resistance of SARS-CoV-2 Mpro E166 variants.

mBio - 9 Jul 2025

Esler Morgan A, Shi Ke, Rollie Joseph A, Delgado Renee, Vishwakarma Jyoti, Dabrowska Agnieszka, Prahlad Janani, Moghadasi Seyed Arad, Harris Reuben S, Aihara Hideki

Abstract excerpt

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) main protease (Mpro) has an essential role in the virus lifecycle and, accordingly, it is a target for antiviral drugs. Multiple studies have identified an Mpro mutation (E166V) that confers strong resistance to clinically relevant inhibitors, including nirmatrelvir, but the underlying mechanism is not fully understood. Here, we report on crystal...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Coronavirus 3C Proteases
Share to COVID-19

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to COVID-19 Drug Treatment

Share to Lactams

Share to Leucine

Share to Nitriles

Share to Proline

Share to SARS-CoV-2

Source

Open in PubMed Open full text

Identifiers

PMID: 40454888
DOI: 10.1128/mbio.02624-24
PMCID: PMC12239574

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural basis for varying drug resistance of SARS-CoV-2 Mpro E166 variants.PMID 40454888Read ↗

Molecular mechanisms of drug resistance and compensation in SARS-CoV-2 main protease: the interplay between E166 and L50.Semantic proximity Read ↗

Novel Mechanisms of SARS-CoV-2 Drug Resistance and Rational Design of Anti-Resistant Antivirals.Semantic proximity Read ↗

Evolutionary and Structural Insights about Potential SARS-CoV-2 Evasion of NirmatrelvirSemantic proximity Read ↗

Molecular mechanisms of SARS-CoV-2 resistance to nirmatrelvir.Semantic proximity Read ↗

Predicting Nirmatrelvir Resistance in SARS-CoV-2 Mpro Mutants with an Integrated Computational Framework.Semantic proximity Read ↗

Naturally Occurring Mutations of SARS-CoV-2 Main Protease Confer Drug Resistance to NirmatrelvirSemantic proximity Read ↗

Naturally occurring mutations of SARS-CoV-2 main protease confer drug resistance to nirmatrelvirSemantic proximity Read ↗

Effects of SARS-CoV-2 Main Protease Mutations at Positions L50, E166, and L167 Rendering Resistance to Covalent and Noncovalent Inhibitors.Semantic proximity Read ↗

Predicting Antiviral Resistance Mutations in SARS-CoV-2 Main Protease with Computational and Experimental Screening.Semantic proximity Read ↗

Functional and Structural Characterization of Treatment-Emergent Nirmatrelvir Resistance Mutations at Low Frequencies in the Main Protease (Mpro) Reveals a Unique Evolutionary Route for SARS-CoV-2 to Gain ResistanceSemantic proximity Read ↗

A comprehensive study of SARS-CoV-2 main protease (Mpro) inhibitor-resistant mutants selected in a VSV-based system.Semantic proximity Read ↗

Changes in the mutational dynamics of the SARS-CoV-2 main-protease substantiate the danger of emerging resistance to antiviral drugs.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.