Article

Characterizing receptor flexibility to predict mutations that lead to human adaptation of influenza hemagglutinin

2020-07-15

Abstract excerpt

A key step in the emergence of human pandemic influenza strains has been a switch in the binding preference of the viral glycoprotein hemagglutinin (HA) from avian to human sialic acid receptors (SAs). The conformation of the bound SA varies substantially with HA sequence, and crystallographic evidence suggests that the bound SA is flexible, so it is difficult to predict from crystal structures which mutations are...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: c6820a35-270d-553f-89b2-fa67d9be8ee5
DOI: 10.1101/2020.07.15.204982

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Characterizing receptor flexibility to predict mutations that lead to human adaptation of influenza hemagglutininDOI 10.1101/2020.07.15.204982Read

Characterizing Receptor Flexibility to Predict Mutations That Lead to Human Adaptation of Influenza Hemagglutinin.Semantic proximity Read

Deep mutational scanning of H5 hemagglutinin to inform influenza virus surveillance.Semantic proximity Read

An airborne transmissible avian influenza H5 hemagglutinin seen at the atomic level.Semantic proximity Read

Host Switching Mutations in H5N1 Influenza Hemagglutinin Suppress Site-specific Activation DynamicsSemantic proximity Read

The structural variability of the influenza A hemagglutinin receptor-binding site.Semantic proximity Read

Insights into the human glycan receptor conformation of 1918 pandemic hemagglutinin-glycan complexes derived from nuclear magnetic resonance and molecular dynamics studies.Semantic proximity Read

Mutation of the second sialic acid-binding site of influenza A virus neuraminidase drives compensatory mutations in hemagglutinin.Semantic proximity Read

Evolution of the receptor binding properties of the influenza A(H3N2) hemagglutininSemantic proximity Read

Combining molecular dynamics with bayesian analysis to predict and evaluate ligand-binding mutations in influenza hemagglutinin.Semantic proximity Read

Diversity of Functionally Permissive Sequences in the Receptor-Binding Site of Influenza Hemagglutinin.Semantic proximity Read

H3N2 influenza A virus gradually adapts to human-type receptor binding and entry specificity after the start of the 1968 pandemicSemantic proximity Read

Structure, Receptor Binding, and Antigenicity of Influenza Virus Hemagglutinins from the 1957 H2N2 PandemicSemantic proximity Read