Ram Sasisekharan, who is currently a professor of Biological Engineering and Health Sciences and Technology at the MIT Massachusetts Institute of Technology (MIT), says that the two mutations in the 1918 influenza strain occurred in a surface molecule called hemagglutinin (HA), which allowed it to bind tightly to receptors in the human upper respiratory tract.
Two mutations dramatically change the HA binding affinity to receptors found in the human upper airways, said Sasisekharan.
In a previous research paper, Sasisekharan and his colleagues had suggested that flu viruses could only bind to human respiratory cells if they matched the shape of sugar (or glycan) receptors found on those cells.
The glycan receptors found in the human respiratory tract are known as alpha 2-6 receptors, and they come in two shapes-one resembling an open umbrella, and another resembling a cone.
That time, the research team said that avian flu viruses must gain the ability to bind to the umbrella-shaped alpha 2-6 receptor to infect humans.
In their current study, they have found that two mutations in HA allow flu viruses to bind tightly or with high affinity to the umbrella-shaped glycan receptors.
The affinity between the influenza virus HA and the glycan receptors appears to be a critical determinant for viral transmission, said Sasisekharan.
With a view to investigating the biochemical basis for hemagglutinin binding to glycans, which leads to viral transmission, the researchers used the 1918 influenza virus as a model system.