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Mystery solved: How poison frogs store their toxins without harming themselves

Researchers have unveiled the identity of a protein responsible for the poison dart frog’s ability to safely accumulate toxins. This discovery solves a long-standing scientific mystery, and also holds promise for potential therapeutic strategies in treating humans poisoned with similar compounds.

Alkaloid compounds and poisonous frogs

Alkaloid compounds, found in everyday consumables such as coffee, tea, and chocolate, contribute to their delightful flavors. However, these compounds can be harmful in large quantities. In humans, the liver effectively breaks down modest amounts of these alkaloids, ensuring their safe metabolism.

In stark contrast, the tiny poison dart frog consumes highly toxic alkaloids in its diet but, rather than breaking them down, uses a unique defense mechanism by accumulating them in its skin as protection against predators.

Lead author Aurora Alvarez-Buylla is a PhD student in the Biology Department at Stanford University in California. She explains the aim of their study, saying, “It has long been a mystery how poison dart frogs can transport highly toxic alkaloids around their bodies without poisoning themselves.”

To investigate this phenomenon, the research team focused on identifying proteins that could safely bind and transport alkaloids in the blood of these remarkable amphibians.

The molecular fishing hook

To unravel the secrets of the poison dart frog, Alvarez-Buylla and her colleagues designed a biochemical ‘molecular fishing hook’ resembling the poison frog’s alkaloid. By using this decoy, they successfully attracted and bound proteins present in blood samples taken from the Diablito poison frog.

This alkaloid-like compound was bioengineered to emit a fluorescent glow under specific light conditions, enabling the team to visually observe the proteins binding to it.

To gain insight into the interaction between proteins and alkaloids, the researchers isolated and studied each protein’s behavior in the presence of these toxic compounds. Astonishingly, they discovered that a specific protein, known as alkaloid binding globulin (ABG), acts as a ‘toxin sponge,’ effectively collecting alkaloids.

Furthermore, they meticulously mapped out the precise binding mechanism of ABG by systematically testing different segments of the protein.

Poisonous frogs and human health

Alvarez-Buylla explains the profound implications of their findings, saying, “The way that ABG binds alkaloids has similarities to the way proteins that transport hormones in human blood bind their targets. This discovery may suggest that the frog’s hormone-handling proteins have evolved the ability to manage alkaloid toxins.”

This intriguing parallel raises the possibility of bioengineering human proteins that can effectively ‘sponge up’ toxins, offering a potentially groundbreaking approach to treat certain types of poisonings.

Senior author Lauren O’Connell, Assistant Professor in the Department of Biology and a member of the prestigious Wu Tsai Neurosciences Institute at Stanford University, highlights the significance of this research.

“Beyond its potential medical relevance, we have achieved a molecular understanding of a fundamental aspect of poison frog biology,” says O’Connell. “This understanding will undoubtedly contribute to future work on studying the biodiversity and evolution of chemical defenses in nature.”

In summary, the identification of the protein responsible for the poison dart frog’s ability to safely accumulate toxins marks a major breakthrough in scientific research. Not only does this discovery shed light on the fascinating mechanisms within the natural world, it also holds potential therapeutic implications for treating human poisonings.

As researchers explore the parallels between the frog’s defense mechanism and human hormone-transporting proteins, we anticipate exciting developments in the field of toxin management and the advancement of innovative therapeutic approaches.

The full study was published in the journal eLife Sciences.


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