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.
Smith says the team traced the source of influenza by homing in
on hemagglutinin, a protein on the surface of the virus that triggers an immune response in our bodies.
Combing the genetic data from a transmission study in ferrets, a team led by Thomas Friedrich, a professor of pathobiological sciences at the University of Wisconsin - Madison School of Veterinary Medicine, found that during transmission, when one animal is infected by another through sneezing or coughing, the process of natural selection acts strongly
on hemagglutinin, the structure the virus uses to attach to and infect host cells.
Not exact matches
A glycoprotein
on the virus's surface called
hemagglutinin, which has 17 identified types (H1 - H17), determines how the virus sticks to and enters the host cell.
Researchers name flu viruses based
on the type of
hemagglutinin (HA) and neuraminidase (NA) proteins they containhence the numbers after «H» and «N» in H5N1.
A designer protein (brown and orange) fits snugly
on top of the influenza virus's
hemagglutinin protein (green), which helps the virus latch onto and infect cells.
In their experimental treatment, he and his colleagues injected mice, ferrets, and monkeys with viral DNA, causing their muscle cells to produce
hemagglutinin, a protein found
on the surface of all flu viruses.
The proteins
hemagglutinin and neuraminidase sit
on the surface of the flu virus.
They target and bind tightly to strain - specific regions of
hemagglutinin (HA) and neuraminidase (NA) proteins
on the virus.
Currently, seasonal flu vaccines are designed to induce high levels of protective antibodies against
hemagglutinin (HA), a protein found
on the surface of the influenza virus that enables the virus to enter a human cell and initiate infection.
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.
Influenza infection begins when
hemagglutinin binds to receptors
on the host cell.
Three mutations in or near
hemagglutinin's binding site (yellow) and one
on its stalk increased transmissibility.
Now, Skehel, along with colleagues at Harvard, Yale, and Emory University in Atlanta, Georgia, has used that sequence to build the virus's
hemagglutinin (HA)-- a protein that latches onto receptors
on the host cell surface — and determine its structure.
ǂ «A stable trimeric influenza
hemagglutinin stem as a broadly protective immunogen» by Impagliazzo et al. published in Science
on Monday 24th August.
The vaccines deliver mRNA encoding for
hemagglutinin to the body's cells, directing them to produce and express this viral antigenic protein transiently
on the cell's surface, much like a native infection would do, but without the ability to cause disease.
* «
Hemagglutinin - stem nanoparticles generate heterosubtypic influenza protection» by Yassine et al. published in Nature Medicine
on Monday 24th August.
The project aims to develop an influenza vaccine that educates the immune system to recognise cross-reactive epitopes by diluting out the strain specific epitope (Epitope Dilution Phenomenon), using a combination of influenza
hemagglutinin antigens delivered
on virus - like particle.
They expressed two versions of
hemagglutinin — one adapted to eggs and one adapted to humans —
on one virus particle.