An Indian-origin researchers at the U.S. Department of Energy's (DOE) Brookhaven National Laboratory has announced that his team has determined the atomic-level structure of a deadly toxin that is often used in cosmetic and therapeutic applications, such as reducing wrinkles and calming a hyperactive bladder.
Brookhaven biologist Subramanyam Swaminathan says that the detailed structure reveals a unique arrangement of the active components that may help understand why botulinum neruotoxin subtype E acts so fast, and thus have implications for improving vaccines and/or therapeutic agents.
"Understanding the differences among the seven botulinum neurotoxin subtypes is particularly imperative at a time of heightened concern about the potential use of these toxins as bioterror weapons," he said.
All seven neurotoxin subtypes cause their deadly effects using a common mechanism, with each step being activated by a different portion, or domain, of the toxin protein.
It binds to a nerve cell, moves into the cell, and cleaves specific proteins that block the release of neurotransmitters, the chemicals nerve cells use to communicate with one another and with muscles.
Without that communication, muscles, including those used to breathe, become paralysed.
"Blocking any of these steps could thwart the toxins' deadly action. But to do that, we need to understand the details of the proteins' structures," Swaminathan said.
He said that his team's findings could help develop faster-acting vaccines and therapeutic agents.
An article on this work has been published in the Journal of Molecular Biology.