This site may earn affiliate commissions from the links on this page. Terms of use.

Amphibian skin is an interesting thing, between the chemicals secreted by the animals themselves and the microbes that thrive on their skin. Poison dart frogs, those neon cuties of the rainforest, are thusly named because their skins secrete a chemical so poisonous that the indigenous people of the Amazon chase down these teensy frogs and rub their hunting darts on them. The skin microbiome of sure amphibians could help us figure out how to curb the fungal epidemic called chytridiomycosis that threatens tropical frogs. Yous've probably heard nearly dogs — and some people! — licking cane toads to obtain a hallucinogenic dose of toad venom. And now an international team of researchers reports that the skin of a common frog produces a chemic with direct virucidal action against a nasty strain of human influenza A.

The chemic is a host-defence peptide that the researchers named urumin, and it'southward produced by a mutual South Indian frog, Hydrophylax bahuvistara. The researchers report that when they exposed homo flu A particles to urumin in the lab, the urumin latched onto the viral particles and physically destroyed them.

Electron micrograph of A) Intact influenza virus particles; B) Remnants of lysed flu virus particles later incubation with urumin. Image: Holthausen, Jacob et al, 2017

It did this by seeking out a unremarkably sheltered place on the virion's surface. The strain of influenza they were using binds to human cells using lollipop-shaped extensions jutting out from its surface. The extensions are made of a protein called hemagglutinin (HA). Unlike strains of the flu take unlike versions of the antigen on the business concern finish of this docking stalk, but the stalk itself tends to be conserved between strains.

Influenza virions, or viral particles.

While the peptide was but active against 1 strain of the flu, the researchers report that information technology did display antiviral activity in vitro and in vivo. In addition to destroying viral particles in the Petri dish, urumin "protected naive mice from lethal influenza infection." When administered intranasally, the peptide protected mice confronting a lethal dose of influenza particles.

The researchers aren't sure of the mechanics by which this peptide destroyed the virus. They hypothesize that electrostatic interactions, like the ones that govern poly peptide folding, are responsible for the sudden destruction. Only since the HA stalk tends to be conserved between strains, if nosotros could figure out how this peptide manages to assault just the stem, it could exist a real pace toward a universal influenza vaccine. Once we know what amino acid sequence enables the peptide to bind to the HA stalk, it becomes possible to utilise technologies like CRISPR to engineer useful peptide variants.

In the concurrently, jokey articles bated, please do not try to treat the cold or influenza past licking frogs.