Researchers at the Scripps Research Institute have used X-ray crystallography to solve the structure of a key protein in Nipah’s pathogenicity. The decoding of the protein’s structure has provided researchers with further information on Nipah’s mechanism of replication. Nipah, which many of you may recognize as the basis for the virus in the film Contagion, is a zoonotic virus capable of causing symptoms ranging from respiratory distress and comas to severe, fatal encephalitis. Currently, there is no vaccine or effective theraputic against the virus, which has an average case fatality rate of 75%.
From Science Daily – “When the scientists solved the crystal structure of the P protein, they found that it forms a tetramer, with four proteins that join to form a single unit. ‘It was surprising to us that this structure is so similar to those from measles and mumps viruses, even though they are only 5 to 26% identical in sequence,’ [first author and researcher Jessica] Bruhn said. ‘If two proteins have high sequence identity then you would expect that they would have similar 3D structures, but to see such similarity in proteins with such low identity was surprising.’ She said this speaks to the importance of structural conservation over sequence conservation — meaning that regardless of whether a protein has an identical sequence of amino acids or not, the structure could still be similar, especially when that structure has the important function of replicating the virus’s RNA genome. ”
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