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Biological Chemistry

Peptide Denies Cell Entry To Ebola Virus

With a newly designed peptide, scientists have developed a way to inhibit the deadly virus

by Stu Borman
April 18, 2011 | A version of this story appeared in Volume 89, Issue 16

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Credit: J. Biol. Chem.
A newly designed peptide prevents the Ebola virus surface glycoprotein shown from adopting this conformation, a shape the glycoprotein must have to catalyze viral fusion with cellular endosomes.
Credit: J. Biol. Chem.
A newly designed peptide prevents the Ebola virus surface glycoprotein shown from adopting this conformation, a shape the glycoprotein must have to catalyze viral fusion with cellular endosomes.

A novel approach to fight Ebola virus uses a designed peptide to inhibit the deadly virus’ entry into host cells. Ebola infection causes a rapidly progressing condition with internal and external bleeding and high fever. The disease has a high mortality rate, and there are currently no approved vaccines or therapies. Infection begins when a viral surface glycoprotein catalyzes fusion between the virus’s membrane and the membrane of endosomes in host cells. C-peptides inhibit similar fusion reactions involving viruses such as HIV and SARS, but they have been ineffective against Ebola. Kartik Chandran and Jonathan R. Lai of Albert Einstein College of Medicine and coworkers have now boosted the activity of Ebola C-peptide by conjugating it to an endosome-targeting sequence (J. Biol. Chem., DOI: 10.1074/jbc.m110.207084). They show that the modified peptide has potent in vitro anti-Ebola activity, and they determined its mechanism of action. The approach “is amenable to targeting other viruses whose fusion intermediates are exposed in the endocytic pathway and will provide a useful suite of research tools to probe intermediates in the process of viral entry,” Lai says.

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