Scientists uncover structure of key pneumonia virus enzyme, suggesting a route for new antiviral treatments

phys.org | 2/22/2018 | Staff
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A team of molecular and structural biologists from Nanyang Technological University, Singapore (NTU Singapore), has found a potential new route to disabling respiratory syncytial virus (RSV) and human metapneumovirus (HMPV) after elucidating the structure of one of its key components.

RSV and HMPV are two closely related viruses causing severe and life-threatening respiratory diseases such as pneumonia and bronchiolitis in premature babies and infants, the elderly, and anyone with a weak immune system.

UNICEF - Pneumonia - Child - World - Seconds

According to UNICEF, pneumonia killed a child somewhere in the world every 39 seconds in 2018, but there are no vaccines or effective antiviral therapies against it.

As they infect human cells, HMPV and RSV commandeer the cell's machinery to make copies of themselves. To initiate the process, special proteins released by the virus interact with each other to make distinct protein complexes.

Nature - Dr - Julien - Lescar - NTU

Writing in Nature, Dr. Julien Lescar from NTU's School of Biological Sciences and his team report that they have used cryo-electron microscopy to image the molecular structure of one of these large complexes, an enzyme called HMPV L:P polymerase.

Cryo-electron microscopy uses an advanced electron-scanning microscope, which can image a cryogenically frozen sample down to the sub-nanometer range. The NTU images captured the enzyme at a resolution of 3.7 Angstrom, or 0.37 nanometers. Based...
(Excerpt) Read more at: phys.org
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