According to researchers at the Monell Center, fruit flies are more like humans in their responses to many sweet tastes than are almost any other species.
The diverse range of molecules that humans experience as sweet do not necessarily taste sweet to other species. For example, aspartame, a sweetener used by humans, does not taste sweet to rats and mice.
However, fruit flies respond positively to most sweeteners preferred by humans, including sweeteners not perceived as sweet by some species of monkeys.
The findings, published in the current issue of the journal Chemical Senses, demonstrate the critical role of environment in shaping the genetic basis of taste preferences and feeding behavior.
“Humans and flies have similar taste responses because they share similar environments and ecological niches, not because their sweet receptors are similar genetically,” notes senior author Paul A.S. Breslin, PhD, a Monell sensory geneticist. “Both are African species, both are omnivorous, and both historically are primarily fruit eaters.”
To compare how molecular structure is related to sweet taste perception in humans and flies, the Monell researchers evaluated how fruit flies respond to 21 nutritive and nonnutritive compounds of varying molecular structure, all of which taste sweet to humans.
Breslin and lead author Beth Gordesky-Gold, PhD, used two behavioral tests to evaluate the flies’ responses to the various sweeteners.
The taste reactivity test measures whether a fly extends its feeding tube, or ‘proboscis,’ to consume a given sweetener. In addition, a two-choice preference test evaluates the flies’ responses to a sweetener by measuring whether they consume it in preference to a control solution (usually water).
The Monell researchers found that fruit flies and humans both respond positively to the same broad range of sweet-tasting molecules.
“The similarity between human and fly responses to sweeteners is astounding, especially in light of the differences in their taste receptors,” notes Gordesky-Gold, a Drosophila (fruit fly) geneticist at Monell.
Sweet receptors belong to a large family of receptors known as G-protein coupled receptors (GPCRs), which are involved in biological processes throughout the body. Human and fly sweet taste GPCRs are presumed to have markedly different structures, an assumption that is based on differences in the genes that code for them.
Since substances will only taste sweet if they are able to bind to and activate a receptor, these two structurally different types of sweet receptors must have similar ‘binding regions’ that fit the same range of molecular shapes.
“That genes could be so divergent in sequence and so similar in physiology and function is truly striking,” says Breslin. “This is a wonderful example of convergent evolution in perceptual behavior, where evolution has taken two different routes to address pressures imposed by shared environment and nutrition.”
Future work will be directed towards modeling how these two structurally different sweet receptors could have highly overlapping sweetener affinities. Such knowledge will increase understanding of how molecules bind to GPCRs, which are targets for many pharmaceutical drugs.
Leslie Stein | EurekAlert!
Show me your leaves - Health check for urban trees
12.12.2017 | Gesellschaft für Ökologie e.V.
Liver Cancer: Lipid Synthesis Promotes Tumor Formation
12.12.2017 | Universität Basel
MPQ scientists achieve long storage times for photonic quantum bits which break the lower bound for direct teleportation in a global quantum network.
Concerning the development of quantum memories for the realization of global quantum networks, scientists of the Quantum Dynamics Division led by Professor...
Researchers have developed a water cloaking concept based on electromagnetic forces that could eliminate an object's wake, greatly reducing its drag while...
Tiny pores at a cell's entryway act as miniature bouncers, letting in some electrically charged atoms--ions--but blocking others. Operating as exquisitely sensitive filters, these "ion channels" play a critical role in biological functions such as muscle contraction and the firing of brain cells.
To rapidly transport the right ions through the cell membrane, the tiny channels rely on a complex interplay between the ions and surrounding molecules,...
The miniaturization of the current technology of storage media is hindered by fundamental limits of quantum mechanics. A new approach consists in using so-called spin-crossover molecules as the smallest possible storage unit. Similar to normal hard drives, these special molecules can save information via their magnetic state. A research team from Kiel University has now managed to successfully place a new class of spin-crossover molecules onto a surface and to improve the molecule’s storage capacity. The storage density of conventional hard drives could therefore theoretically be increased by more than one hundred fold. The study has been published in the scientific journal Nano Letters.
Over the past few years, the building blocks of storage media have gotten ever smaller. But further miniaturization of the current technology is hindered by...
With innovative experiments, researchers at the Helmholtz-Zentrums Geesthacht and the Technical University Hamburg unravel why tiny metallic structures are extremely strong
Light-weight and simultaneously strong – porous metallic nanomaterials promise interesting applications as, for instance, for future aeroplanes with enhanced...
11.12.2017 | Event News
08.12.2017 | Event News
07.12.2017 | Event News
12.12.2017 | Physics and Astronomy
12.12.2017 | Earth Sciences
12.12.2017 | Power and Electrical Engineering