Northwestern University researchers have, for the first time, determined the 3D atomic structure of a key complex in paramyxoviruses, a family of viruses that includes measles, mumps, human parainfluenza and respiratory syncytial virus (RSV).
This information could help others design and develop antiviral drugs for these viruses as well as for coronavirus, which functions similarly to paramyxoviruses.
"This takes some of the guesswork out of designing drugs," said Northwestern's Robert Lamb, who co-led the study. "Traditionally, you have to develop drugs randomly and hope you hit a target, but it doesn't happen very often."
To find the unique structure, researchers used cryogenic electron microscopy (cryo-EM). The relatively new technique enables researchers to peer inside molecules to determine the 3D shape of proteins, which are often thousands of times smaller than the width of a human hair. Before cryo-EM, researchers mainly used X-ray crystallography, which is incapable of capturing high-resolution images of this enzyme. Called a polymerase, the enzyme assembles RNA molecules.
"Crystallography only works for very orderly and organized proteins," said Northwestern's Yuan He, who co-led the study. "Virus polymerase complexes are too big to be crystallized and don't have uniformity."
The study will be published on Feb. 17 in the Proceedings of the National Academy of Sciences .
Lamb is the Kenneth F. Burgess Professor of Molecular Biosciences in Northwestern's Weinberg College of Arts and Sciences and an investigator of the Howard Hughes Medical Institute. Yuan He is an assistant professor of molecular biosciences in Weinberg.
Although the first documented case of mumps occurred in the 5th century and measles in the 9th century, researchers did not have the equipment to characterize their atomic structures until relatively recently. A trio of biophysicists received the 2017 Nobel Prize in Chemistry for developing cryo-EM, which ultimately opened the door for Lamb and He. Related Stories
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