(New York, New York) -- Modest changes in the 1918 flu virus's hemagglutinin receptor binding sitea molecular structure critical for the spread of infectionstopped viral transmission in ferrets, according to a new study conducted by researchers at Mount Sinai School of Medicine and at the Centers for Disease Control and Prevention. The finding, published in the February 1 issue of Science, could have significant clinical implications in helping scientists develop ways to break the disease cycle and possibly help reduce the risk for a potential pandemic.
While flu pandemics occur every 10 to 40 years, the factors that lead to the emergence of pandemic viruses are not well understood, explains study co-author Adolfo Garca-Sastre, PhD, Professor of Microbiology at Mount Sinai School of Medicine. "What's most threatening is the possibility of another pandemic, similar to that of 1918, which was caused by a novel influenza subtype virus capable of causing severe respiratory disease and death," says Dr. Garca-Sastre. "So if we can understand the molecular mechanisms behind its transmission, perhaps we can do something to block transmission and prevent illness."
To do this, Dr. Garca-Sastre and his team studied two key molecular structures: hemagglutinin, a protein located in of the surface of the influenza virus, and sialic acid, a cellular molecule that is recognized by hemaglutinins of both human and avian strains of influenza virus. These molecules are key to initiation of infection. There are 16 different subtypes of hemagglutinin called H1 through H16, present in influenza virus strains circulating in birds. H1 and H3 are found today in human influenza viruses.
Hemaglutinin helps open the door to the cell to allow the virus to infect. The first step is in this process is the binding of the hemagglutinin to sialic acid containing molecules in the cell surface. There are two primary ways sialic acids are associated with molecules in t
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