Papua, New Guinea is notorious for its heritage of brain-eating cannibal tribes, such as the Asmat and the Fore. Now, scientists are studying the descendents of these mind-munchers to help develop a treatment for mad cow disease.
Researchers are concentrating on the Fore tribe of the Eastern Highlands. The natives used to scarf down the brains of dead relatives in elaborate rituals. Unfortunately, this practice led to the spread of a brain disease similar to mad cow that threatened the population.
Brain consumption has been outlawed since the 1950′s. Since then, the tribe has undergone a rapid genetic mutation that protects against the disease, called kuru, thereby eliminating the threat to survival. Kuru is caused by prions: brain proteins that exhibit unusual shapes. Prions are also responsible for mad cow disease.
The research was reported in the New England Journal of Medicine by Dr. Simon Mead of the Medical Research Council Prion Unit located at University College in London. By studying the protecting mutation, the researchers hope to come up with a treatment for kuru and related diseases.
Kuru used to be a feared killer that wiped out whole female populations of tribal women in Papua. It was the women who ritually ate the brains of dead tribe members. Some of these women developed a protective gene which shielded them from kuru and helped them live to ripe old ages. Women who lacked the gene died young.
Dr. Mead points out that this is an example of human evolution. His study of over 3,000 tribespeople included 709 noggin-nibblers, of whom 152 died of kuru. Examination of the prion genes found a mutation called G127V that served to protect the natives from kuru. The gene was spread through natural selection.
“It is remarkable how few definite examples there are that we can really link with a clear history of a disease or an event. It was such a devastating disease and well-documented … and we can now see the effects of this genetically,” Dr Mead said.
The G127V mutation prevents misshapen prions from attaching to healthy prions, thus preventing the disease. Knowing the attachment point for the prions could lead to treatments to inhibit the disease.
“If you could find a drug or a molecule or an antibody that binds to that site, you could interfere with that process,” Dr Mead said.