A synthetic molecule that imitates an important section of the Ebola virus promises to speed up discovery of anti-Ebola agents capable of dealing with all current strains and any that emerge in future epidemics.

The molecule – known as a peptide mimic – represents a critical region of the Ebola virus that does not change as it mutates. This means it can be used as a universal drug target for rapid screening of drugs effective against all strains of the virus.

A study describing the development and testing of the new molecule is published in the journal Protein Science.

The work – which involved a large team of researchers – was led by biochemists at the University of Utah in Salt Lake City and was funded by the National Institutes of Health.

Ebola is a deadly virus that causes hemorrhagic fever and – depending on which of the five known strains is involved – kills between 5-9 out of every 10 people it infects.

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Ebola virus disease causes hemorrhagic fever and has been occurring more frequently, particularly in West Africa.

Outbreaks of Ebola virus disease have been occurring more and more frequently in recent years. The current epidemic in West Africa is unprecedented in terms of the scale and speed of its devastation; it is has become an urgent global health problem.

There are currently no approved anti-Ebola drugs, although a number of experimental drugs that target the Zaire strain behind the current outbreak in West Africa are being fast-tracked through clinical trials.

But co-lead investigator Debra Eckert, research assistant professor of biochemistry at the University of Utah, warns that while these trial drugs will hopefully lead to an effective treatment for people affected by the current epidemic, they are unlikely to be effective in future outbreaks caused by different or new species of Ebola. She urges:

“Development of a broadly acting therapy is an important long-term goal that would allow cost-effective stockpiling of a universal Ebola treatment.”

The new peptide molecule that Prof. Eckert and colleagues have developed mimics a highly conserved region of an Ebola protein that controls how the virus enters the human host cell, which marks the start of the infection process.

In their study report, they describe how the synthetic peptide can be used in high-throughput drug screens, aiding rapid identification of potential anti-Ebola agents from billions of possible drug candidates.

Another huge advantage of the new molecule is that unlike many of the drugs currently being tested against Ebola, it can be used to find drugs that work against all current and future strains of the virus.

Lead author Dr. Tracy R. Clinton says the current Ebola epidemic shows the need for effective broad-spectrum therapies, and adds:

Importantly, viral sequence information from the epidemic reveals rapid changes in the viral genome, while our target sequence remains the same. Therefore, our target will enable the discovery of drugs with the potential to treat any future epidemic, even if new Ebola virus strains emerge.”

The new molecule is already being used to screen for anti-Ebola drugs. The screening is being carried out at Navigen, a Salt Lake City pharmaceutical discovery and development company, two members of which were on the study team.

Meanwhile, Medical News Today recently brought news of a crystallography study that proposed an Ebola protein important for virus replication as a drug target.