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Virus Can Mutate lethally With Help Of Carbohydrates

protein shells were different by only 14 out of more than 500 amino acids. They also found that a couple of years back these normally mild MVMp viruses mutated quite suddenly and became harmful to the defenseless mice.

Agbandje-McKenna, who is associated with both UF's McKnight Brain Institute and the UF Genetic Institute explained “One or two changes in amino acids made the difference between a virus that kills and one that does not kill mice. We wanted to know how such a slight change could make this virus become lethal.” An international team of more than 230 scientists under the National Institute of General Medical Sciences, the UF researchers working with the Consortium for Functional Glycomics, had become the first to use a new technique called a glycans array to study how a whole, intact virus interacts with carbohydrates.

The scientist’s explained to have exposed 189 glycans that were mounted on a 3-by- 5-inch plastic plate to dangerous MVMi, harmless MVMp and three potentially dangerous, mutant strains of MVMp. They claimed to have found that the MVMp proteins stuck to the same three glycans on the plate. However, one of the mutant MVMp viruses also bound to an additional glycan and that one was associated with the more dangerous MVMi strain.

She said, “A single amino-acid change in the virus' protein shell changes how it can grip the cell, making it more deadly. Actually, the affinity is reduced, so the more deadly strain of the virus actually does not bind as tightly. We're not sure why, but it may be because it can more easily let go and get into the cell to cause disease. It's not giving the body the time to mount an immune response.” The scientists were of the opinion that on understanding as to how viruses adapt to different hosts and different tissues could be useful for developing gene therapies, which involve introducing specially engineered genes into a patient's cells through the apparently harmless vir
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