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

Permissive secondary mutations enable the evolution of influenza oseltamivir resistance.

Science (New York, N.Y.) - 4 Jun 2010

Bloom Jesse D, Gong Lizhi Ian, Baltimore David

Abstract excerpt

The His274-->Tyr274 (H274Y) mutation confers oseltamivir resistance on N1 influenza neuraminidase but had long been thought to compromise viral fitness. However, beginning in 2007-2008, viruses containing H274Y rapidly became predominant among human seasonal H1N1 isolates. We show that H274Y decreases the amount of neuraminidase that reaches the cell surface and that this defect can be counteracted by secondary...

Read the complete abstract on PubMed

Topics

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

Share to Antiviral Agents
Share to Drug Resistance, Viral
Share to Genes, Viral

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Genetic Fitness

Share to Influenza A Virus, H1N1 Subtype

Share to Influenza, Human

Share to Neuraminidase

Share to Oseltamivir

Source

Open in PubMed Open full text

Identifiers

PMID: 20522774
DOI: 10.1126/science.1187816
PMCID: PMC2913718

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Permissive secondary mutations enable the evolution of influenza oseltamivir resistance.PMID 20522774Read ↗

Identification of a Permissive Secondary Mutation That Restores the Enzymatic Activity of Oseltamivir Resistance Mutation H275Y.Semantic proximity Read ↗

A computational-experimental approach identifies mutations that enhance surface expression of an oseltamivir-resistant influenza neuraminidase.Semantic proximity Read ↗

Oseltamivir-resistant influenza A(H1N1)pdm2009 strains found in Brazil are endowed with permissive mutations, which compensate the loss of fitness imposed by antiviral resistance.Semantic proximity Read ↗

Predicting Permissive Mutations That Improve the Fitness of A(H1N1)pdm09 Viruses Bearing the H275Y Neuraminidase Substitution.Semantic proximity Read ↗

Amino Acid Changes in Hemagglutinin Contribute to the Replication of Oseltamivir-Resistant H1N1 Influenza VirusesSemantic proximity Read ↗

Pandemic H1N1 2009 influenza virus with the H275Y oseltamivir resistance neuraminidase mutation shows a small compromise in enzyme activity and viral fitnessSemantic proximity Read ↗

H274Y's Effect on Oseltamivir Resistance: What Happens Before the Drug Enters the Binding Site.Semantic proximity Read ↗

Molecular mechanism of the enhanced viral fitness contributed by secondary mutations in the hemagglutinin protein of oseltamivir resistant H1N1 influenza viruses: modeling studies of antibody and receptor binding.Semantic proximity Read ↗

Oseltamivir resistance and the H274Y neuraminidase mutation in seasonal, pandemic and highly pathogenic influenza viruses.Semantic proximity Read ↗

Detection of the rapid emergence of the H275Y mutation associated with oseltamivir resistance in severe pandemic influenza virus A/H1N1 09 infectionsSemantic proximity Read ↗

Role of permissive neuraminidase mutations in influenza A/Brisbane/59/2007-like (H1N1) viruses.Semantic proximity Read ↗

Influenza neuraminidase inhibitors: antiviral action and mechanisms of resistanceSemantic proximity Read ↗

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