scispace - formally typeset
Journal ArticleDOI

Substitutions near the receptor binding site determine major antigenic change during influenza virus evolution.

TLDR
The findings of Koel et al. (p. 976) show that major antigenic change can be caused by single amino acid substitutions, which substantially skew the way the immune system “sees” the virus.
Abstract
The molecular basis of antigenic drift was determined for the hemagglutinin (HA) of human influenza A/H3N2 virus. From 1968 to 2003, antigenic change was caused mainly by single amino acid substitutions, which occurred at only seven positions in HA immediately adjacent to the receptor binding site. Most of these substitutions were involved in antigenic change more than once. Equivalent positions were responsible for the recent antigenic changes of influenza B and A/H1N1 viruses. Substitution of a single amino acid at one of these positions substantially changed the virus-specific antibody response in infected ferrets. These findings have potentially far-reaching consequences for understanding the evolutionary mechanisms that govern influenza viruses.

read more

Citations
More filters
Journal ArticleDOI

The evolution of seasonal influenza viruses

TL;DR: Recent advances in understanding the molecular determinants of influenza virus immune escape, sources of evolutionary selection pressure, population dynamics of influenza viruses and prospects for better influenza virus control are discussed.
Journal ArticleDOI

Contemporary H3N2 influenza viruses have a glycosylation site that alters binding of antibodies elicited by egg-adapted vaccine strains.

TL;DR: The data suggest that influenza virus antigens prepared via systems not reliant on egg adaptations are more likely to elicit protective antibody responses that are not affected by glycosylation of antigenic site B of H3N2 HA.
References
More filters
Journal ArticleDOI

Receptor Binding and Membrane Fusion in Virus Entry: The Influenza Hemagglutinin

TL;DR: Comparisons to the soluble N-ethyl-maleimide-sensitive factor attachment protein receptor (SNARE) protein complex of vesicle fusion suggests that these molecules are all in the fusion-activated conformation and that the juxtaposition of the membrane anchor and fusion peptide, a recurring feature, is involved in the fused mechanism.
Journal ArticleDOI

Mapping the Antigenic and Genetic Evolution of Influenza Virus

TL;DR: The antigenic evolution of influenza A (H3N2) virus was quantified and visualized from its introduction into humans in 1968 to 2003 and offers a route to predicting the relative success of emerging strains.
Journal ArticleDOI

Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation

TL;DR: Four ‘antigenic sites’ on the three-dimensional structure of the influenza haemagglutinin are identified and at least one amino acid substitution in each site seems to be required for the production of new epidemic strains between 1968 and 1975.
Journal ArticleDOI

A DNA transfection system for generation of influenza A virus from eight plasmids

TL;DR: An eight-plasmid DNA transfection system for the rescue of infectious influenza A virus from cloned cDNA facilitates the design and recovery of both recombinant and reassortant influenza A viruses, and may also be applicable to the recovery of other RNA viruses entirely from cloning cDNA.
Journal ArticleDOI

Structural and Functional Bases for Broad-Spectrum Neutralization of Avian and Human Influenza A Viruses

TL;DR: The crystal structure of one such nAb bound to H5 shows that it blocks infection by inserting its heavy chain into a conserved pocket in the stem region, thus preventing membrane fusion, and suggests that nAb-based immunotherapy is a promising strategy for broad-spectrum protection against seasonal and pandemic influenza viruses.
Related Papers (5)