New species of stegosaur
A new species of stegosaur – named Bashanosaurus primitivus – has been uncovered in China and researchers say that it’s one of the earliest stegosaurs ever found. It roamed the earth around 168 million years ago during the Middle Jurassic period, much earlier than most known stegosaurs, according to a new study.
“Bashan” is the ancient name for the area of Chongqing in China where the stegosaur was found; the Latin “primitivus” means “first”.
The fossilised remains suggest that the animal discovered measured 2.8 metres from nose to tail, but it’s unclear whether it was an adult or juvenile.
The ancient stegosaur has armour plates with a narrower and thicker base than other stegosaurs and has similarities with some of the first armoured dinosaurs, which are over 20 million years older. This new find, published in the Journal of Vertebrate Paleontology, suggests that stegosaurs may have originated in what is now modern-day Asia.
Mummies were made earlier than thought in Europe
New analysis of 8,000-year-old hunter-gatherer burial sites in the Sado Valley, Portugal, has found evidence of mummification roughly a thousand years earlier than the previous oldest intentionally mummified remains, found in the Atacama Desert in Chile.
The research team used photographs of remains excavated in the 1960s, and applied a technique called archaeoathanology, which involves combining observations of the positioning of the bones with knowledge about how the body decomposes under different conditions; with it, you can tell how a body was treated after death and before burial.
It’s the first evidence for deliberate mummification in Mesolithic Europe. The study was published in the European Journal of Archeology.
Mussels’ underwater glue inspires synthetic cement
If you’ve ever tried to pry mussels away from a surface you’d know how near-impossible it is to do. Scientists have tried for years to replicate mussels’ extraordinary adhesive and its properties in the lab, by targeting some of the eight proteins that the bivalves secrete. These proteins coat an organ called a foot that’s use to attach to surfaces.
Now, researchers have created a material that performs even better than the substance they were trying to mimic. They’ve used a new method, in which they arrange strands of one of the protein’s amino-acid building blocks in parallel on a synthetic polymer backbone. This results in something that looks like a brush of amino acids – rather than joining them in a straight line, as a chain.
Then they applied either the new protein-like polymer (PLP) or the native mussel protein to glass plates and placed cells on the plates to assess how many were still present after washing. The new PLP formed a cellular superglue, leaving the most cells attached.
“The polymer could be used as an adhesive in a biomedical context, which means now you could stick it to a specific tissue in the body,” says author Nathan Gianneschi, professor of chemistry at Northwestern University in the US. “And keep other molecules nearby in one place, which would be useful in wound healing or repair.”
The study was published in the Journal of the American Chemical Society.
Gene editing gets safer thanks to redesigned Cas9 protein
One of the greatest challenges with using CRISPR-based gene editing in humans is that it sometimes makes changes to the wrong section of the genome; it’s possible to accidentally create a dangerous new mutation in one spot in the genome while trying to repair an existing mutation in another.
Now, scientists have redesigned a key component of the widely used CRISPR-based gene editing tool – the enzyme Cas9 that cuts DNA at a specific location so that bits of DNA can be added or removed – to be 4,000 times less likely to target the wrong stretch of DNA.
According to the new study, published in Nature, this is the first successful attempt at redesigning Cas9 to be more accurate that doesn’t also sacrifice the speed at which it does its job – the researchers have called it SuperFi-Cas9.
They did this by developing a new technique. It uses cryo-electron microscopy to take snapshots of Cas9 in action as it interacts with mismatched DNA that isn’t the correct sequence being sought. From this the researchers were able to identify a “finger” of the protein that normally works to stabilise mismatched DNA, and redesigned it to instead be pushed away from the DNA. This prevents Cas9 from continuing the process of cutting and editing the wrong sequence.
So far, this has only been demonstrated in test tubes but there are plans to test in living cells.
Australian bull ant venom could be used to target pain
Australian bull ants have evolved a venom molecule perfectly designed to target one of their predators – the echidna – that also could have implications for people with long-term pain, according to a new Australian study.
Researchers from the University of Queensland (UQ) found a bull ant venom component that exploits a pain pathway in mammals. By searching databases for similar amino acid sequences, they found that the venom molecule matched that of mammalian hormones related to Epidermal Growth Factor (EGF) – a protein that stimulates cell growth.
The venom doesn’t work by causing immediate pain but instead binds to EGF receptors, causing long-lasting hypersensitivity to pain.
EGF-inhibitor drugs are already available on the market as anti-cancer therapies to slow tumour growth, with evidence suggesting that patients who take them experience less long-term pain. The team hopes that this research, published in PNAS, will inspire new ways to treat long-term pain.
“We hope that by highlighting the role of this signalling pathway in pain, we can encourage different strategies for pain treatment, especially long-term pain for which treatment is currently limited,” says Dr Sam Robinson, from UQ’s Institute for Molecular Bioscience.
Imma Perfetto is a science journalist at Cosmos. She has a Bachelor of Science with Honours in Science Communication from the University of Adelaide.
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