A transmission electron micrograph of Nipah virions isolated from a patient's cerebrospinal fluidWIKIMEDIA, CDCThe Nipah virus phosphoprotein, P, plays a key role in viral replication. Therefore, understanding its structure may shed light on ways to disrupt the viral life cycle. “If you can prevent the virus from making more RNA, then it can’t replicate, which is a good strategy for developing antiviral medications,” Jessica Bruhn, a graduate student in Erica Ollmann Saphire’s lab at Scripps Research Institute in La Jolla, California, said in a press release.
With this in mind, Bruhn, Saphire, and colleagues subjected the protein to X-ray crystallography, observing diffraction patterns that revealed its shape: “a long, parallel, tetrameric, coiled coil with a small, α-helical cap structure,” according the paper published in the December issue of the Journal of Virology. Interestingly, this shape is highly similar to the P protein structure of the sendai, measles, and mumps paramyxoviruses, all of which are long, tetrameric coils, despite the fact that these viruses share little sequence identity with one another or with Nipah.
“It was surprising to us that this structure is so similar to those from measles and mumps viruses, even though they are only 5 [percent] to 26 percent identical in sequence,” Bruhn said in the release. The results ...
