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During the 1918 pandemic outbreak, two mutations in the H1N1 avian flu virus were critical for viral transmission in humans that killed at least 50 million people.
Ram Sasisekharan, the Underwood Prescott Professor of Biological Engineering and Health Sciences and Technology mentioned that, two mutations dramatically change the HA binding affinity to receptors found in the human upper airways. The 1918 influenza strain developed two mutations in a surface molecule called hemagglutinin (HA), which allowed it to bind tightly to receptors in the human upper respiratory tract.
Flu viruses known can only bind to human respiratory cells if they match the shape of sugar (or glycan) receptors found on those cells. To infect humans, it is found that avian flu viruses must gain the ability to bind to the umbrella-shaped alpha 2-6 receptor, the glycan receptors found in the human respiratory tract.
Current study showed that two mutations in HA allow flu viruses to bind tightly or with high affinity to the umbrella-shaped glycan receptors, and this appears to be a critical determinant for viral transmission.
Hopefully, this research could aid researchers to monitoring the HA mutations of H5N1 avian flu strains in Asia.
Adapted from materials provided by Massachusetts Institute of Technology. Enriched from ScienceDaily
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