Influenza infection begins when
hemagglutinin binds to receptors on the host cell.
Hemagglutinin binds to glycan receptors found on the surface of respiratory cells, and the strength of that binding determines how effectively the virus can infect those cells.
Not exact matches
The effort is complicated because there are some 16 types of key surface proteins (
hemagglutinin) that help the virus
bind to host cells, in addition to the several varieties of viral neuraminidase proteins.
In escaping the immune system, the new mutations can inadvertently disrupt this golden
binding point, which can be remedied by adding a sugar molecules in the just the part of the
hemagglutinin.
They target and
bind tightly to strain - specific regions of
hemagglutinin (HA) and neuraminidase (NA) proteins on the virus.
Using a crystal structure of a complex protein compound of botulinum neurotoxin, Rongsheng Jin, associate professor of physiology & biophysics at UC Irvine, and collaborators found that these compounds — called clostridial
hemagglutinin (HA)--
bind with epithelial cell proteins in the intestines of patients, which initiates a process that disrupts the close intercellular seals so that the complex toxin molecules can slip through the epithelial barrier.
Another mutation, in the T200A position, allows
hemagglutinin to
bind more strongly to glycan receptors, making the virus more infectious.
Hemagglutinin, which plays a role in how the virus
binds to host cells, has 18 known types; neuraminidase, which helps the virus detach from the cell so it can spread through the body, has 11.
Three mutations in or near
hemagglutinin's
binding site (yellow) and one on its stalk increased transmissibility.
He notes, for example, his lab's surprising finding that the mutations connected to transmission do not simply involve the way influenza's
hemagglutinin protein
binds to cellular receptors, as many researchers assume.
Using a combination of laboratory assays and computer algorithms, the team tested various mutations in HB36.5, looking for single amino acid changes that would increase how tightly the protein
bound to a diverse group of
hemagglutinins.
Wilson's laboratory used X-ray crystallography to determine the atomic structures of the H7N9
hemagglutinin protein
bound to these sialic acid receptor molecules.
This image from the work shows the
binding of avian - like glycan receptors (yellow spheres) to the 2013 H7N9 influenza virus
hemagglutinin (in ribbon diagram).
Paulson's team — including postdoctoral fellows Robert P. de Vries and Corwin M. Nycholat and Research Assistant Ryan McBride — tested the ability of the virus's
hemagglutinin (HA) protein, to
bind to different human and avian receptor variants.
To address this question, Sasisekharan and his team analyzed the structure of the H5N1 and H7N9 viruses, focusing on
hemagglutinin (HA)-- a type of viral protein that
binds to cell receptors in the respiratory tract of hosts.
The gene, called H5, is one of 16 subtypes of
hemagglutinin, a protein that
binds the avian influenza virus to the cells it infects.
A small - molecule fragment that emulates
binding of receptor and broadly neutralizing antibodies to influenza A
hemagglutinin
Hemagglutinin homologue from H17N10 bat influenza virus exhibits divergent receptor -
binding and pH - dependent fusion activities.