By engineering a peptide that can prevent the attachment of human parainfluenza viruses (HPIVs) to cells, researchers have improved a method in rodent models intended to help keep children healthy. HPIVs are the leading cause of childhood respiratory infections, responsible for 30% to 40% of illnesses like croup and pneumonia. The viruses also affect the elderly and people with compromised immune systems. To sicken people, HPIVs must latch onto cells and inject their genetic material to start making new viruses. HPIV3 is the most prevalent among these viruses. There are currently no approved vaccines or antivirals for HPIV3 infection in people. In a study led by the Sam Gellman (photo), PhD, lab in the Chemistry Department at the University of Wisconsin-Madison, and the lab of Anne Moscona, MD, and Matteo Porotto, PhD, at Columbia University, researchers built upon years of work on peptide treatments to generate one capable of blocking the HPIV3 attachment process. The researchers’ work was published online on April 7, 2021 in the Journal of the American Chemical Society. The article is titled “Engineering Protease-Resistant Peptides to Inhibit Human Parainfluenza Viral Respiratory Infection” (https://pubs.acs.org/doi/10.1021/jacs.1c01565). To enter host cells, HPIVs use specialized fusion proteins that resemble three corkscrews laid side-by-side. Earlier work by the the Moscona-Porotto lab showed that scientists could derive a partial chunk of this corkscrew protein from HPIV3, introduce this peptide to the virus, and prevent the corkscrew from driving the infection process. The peptide, itself a corkscrew, essentially zippers up with the virus's corkscrews, creating a tight bundle of six corkscrew shapes. The newly modified peptide persists longer in the body, making it about three times more effective at blocking infection in rodent models of disease than the original form.
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