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  • Malaria's 'surprising' proteins could aid drug search


Recent malaria research — so intriguing that the scientists who conducted it did not initially believe their findings — could aid efforts to develop drugs or vaccines against the deadliest form of the disease.

The study, published today (3 November) in Nature revealed that the way proteins made by the parasite Plasmodium falciparum interact with each other is almost totally different to the way proteins made by other organisms do.

The researchers, based at the University of California at San Diego, United States, had previously shown that species as distinct as fruit flies, microscopic worms and yeasts not only have hundreds of proteins in common, but also use them in similar ways.

Lead researcher Trey Ideker say that because of this similarity, the team "didn't initially believe our own analysis, which showed that there are only three Plasmodium protein interactions in common with yeast and none in common with the other species studied".

Although humans and P. falciparum share many proteins in common, within each species the proteins can interact in different ways, meaning that similar proteins could have entirely different functions in the parasite and its host, says co-author Taylor Sittler.

The research means that scientists might now have many more avenues to explore in their search for a first malaria vaccine or new drugs to combat the parasite, which is showing growing resistance to existing drugs such as chloroquine.

By knowing that certain malaria proteins are involved in the parasite's invasion of human red blood cells, says Sittler, "you can surmise that proteins interacting with those proteins are also involved."

P. falciparum causes more than 90 per cent of all human deaths from malaria, killing up to 2.7 million people every year, according to the World Health Organization.

Sittler and colleagues based their analysis on data published by Douglas LaCount of the US-based Howard Hughes Medical Institute and colleagues in the same issue of Nature.

Link to full paper in Nature

Reference: Nature 438, 108 (2005)

Link to full paper by LaCount and colleagues in Nature

Reference: Nature 438, 103 (2005)

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