The structure and function of a protein playing a vital role in the life of a parasite resulting in the killing of 655,000 people in 2010 has been cracked by Scientists at the Washington University.
The protein is an enzyme that Plasmodium falciparum, the protozoan that causes the most lethal form of malaria, uses to make cell membrane.
The protozoan cannot survive without this enzyme, but even though the enzyme has many look-alikes in other organisms, people do not make it.
Together these characteristics make the enzyme an ideal target for new anti-malarial drugs.
The protein's structure might have remained an enigma, had it not been the "unreasonable optimism" of Joseph Jez, PhD, associate professor of biology in Arts and Sciences, which carried his team through a six-year-long obstacle course of failures and setbacks.
"What my lab does is crystallize proteins so that we can see what they look like in three dimensions," Jez said.
"The idea is that if we know a protein's structure, it will be easier to design chemicals that would target the protein's active site and shut it down," he added.
One of the proteins Lee worked with is made by Haemonchus contortus, or the Barber's pole worm, a veterinary parasite that attaches itself to the lining of the stomach of a ruminant such as a sheep and feeds on its blood, leaving the animal emaciated and anemic.
The research was published in the January 6 issue of the Journal of Biological Chemistry (JBC).