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Drugs, Vaccines and Therapeutics
, Genomics, Proteomics and Bioinformatics
, Microbiology
by ruth on December 21, 2007

... Drs. Porotto and Moscona knew that when the receptor-binding molecule on the virus-simply called "G"-binds to the surface of the cell, it activates a special "fusion protein." This fusion molecule has to then undergo some shape changes to turn itself into a six-helix bundle. Once that's done, it helps the virus fuse with, and enter, the cell, Dr. Porotto explains.
However, the Weill Cornell team discovered that a peptide specific to the parainfluenza virus "fusion protein" ("F") can inhibit this shape-changing step-stopping fusion cold.
"Surprisingly, this parainfluenza F-peptide turned out to be even more effective at inhibiting Hendra virus fusion than peptides derived from the Hendra virus itself," Dr. Moscona says. "It also appears to do much the same thing with the Nipah virus, inhibiting fusion there, too."
Experiments on monkey cells have shown that the peptide effectively blocked infection with both live Hendra and Nipah. The findings have been published recently in the Journal of Virology.
Source: Weill Cornell Medical College
Permalink: Peptide Drug Aimed at Two Bioterror Agents
Tags:
bioterrorism
bioterror
biohazard
viruses
drug+discovery
outbreak
epidemic
drug
bioterror+agents
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