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

Impact of the polymerase acidic protein E199K substitution in influenza A viruses on baloxavir susceptibility

3 May 2025

Abstract excerpt

Baloxavir marboxil, a cap-dependent endonuclease inhibitor, was approved in Japan in 2018 for the treatment and prophylaxis of influenza. Its active form, baloxavir acid, binds to the polymerase acidic (PA) protein endonuclease domain, inhibiting viral RNA cleavage. PA substitutions (e.g., E23K, I38T, E199G) have been associated with reduced susceptibility to baloxavir. During nationwide monitoring in Japan, we...

Topics

Join the communities discussing this publication.

Herpesvirus Infections and Treatments
Influenza Virus Research Studies
Virus-based gene therapy research

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 40324596
DOI: 10.1016/j.antiviral.2025.106173

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Impact of the polymerase acidic protein E199K substitution in influenza A viruses on baloxavir susceptibilityPMID 40324596Read ↗

Baloxavir susceptibility of seasonal influenza viruses during the first seven seasons of clinical use in Japan, 2017/18 to 2023/24.Semantic proximity Read ↗

Detection of influenza A(H3N2) viruses with polymerase acidic subunit substitutions after and prior to baloxavir marboxil treatment during the 2022–2023 influenza season in JapanSemantic proximity Read ↗

Global update on the susceptibilities of human influenza viruses to neuraminidase inhibitors and the cap-dependent endonuclease inhibitor baloxavir, 2017-2018.Semantic proximity Read ↗

PA-E18G substitution in influenza A virus confers resistance to ZX-7101, a cap-dependent endonuclease inhibitorSemantic proximity Read ↗

A Sequence-Based Update on Amino Acid Substitutions in Influenza Polymerase Acidic Protein in Europe That Alter Baloxavir Susceptibility From 2009 to 2025.Semantic proximity Read ↗

Influenza A virus polymerase acidic protein E23G/K substitutions weaken key baloxavir drug-binding contacts with minimal impact on replication and transmissionSemantic proximity Read ↗

Comprehensive assessment of amino acid substitutions in the trimeric RNA polymerase complex of influenza A virus detected in clinical trials of baloxavir marboxilSemantic proximity Read ↗

Treatment-Emergent Influenza Virus Polymerase Acidic Substitutions Independent of Those at I38 Associated With Reduced Baloxavir Susceptibility and Virus Rebound in Trials of Baloxavir Marboxil.Semantic proximity Read ↗

A community cluster of influenza A(H3N2) virus infection with reduced susceptibility to baloxavir due to a PA E199G substitution in Japan, February to March 2023Semantic proximity Read ↗

Emergence of the novel PA-D27G mutation conferring reduced baloxavir susceptibility in influenza A viruses circulating in China, 2018-2025.Semantic proximity Read ↗

Genotypic and phenotypic susceptibility of emerging avian influenza A viruses to neuraminidase and cap-dependent endonuclease inhibitors.Semantic proximity Read ↗

Impact of Baloxavir Resistance-Associated Substitutions on Influenza Virus Growth and Drug Susceptibility.Semantic proximity Read ↗

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