What makes certain groups more vulnerable to COVID-19? Researchers look to animals to find clues in proteins involved in infection — ScienceDaily

What makes the elderly and people with underlying conditions more vulnerable to COVID-19? According to a new study led by McGill University researchers, clues can be found in the proteins involved in initiating infection, as the virus binds to host cells of different animals. Greater cellular oxidation with aging and sickness may explain why seniors and people with chronic illness get infected more often and more severely.

Over 60 million people have been infected and around 1.5 million have died from COVID-19. The virus is disrupting economies and food supply chains all over the world. Understanding why some animals get infected and others do not could be the key to unlocking new treatments and therapies. In a study published in Computational and Structural Biotechnology Journal, researchers analyzed available protein sequences of the virus and host cell receptors across different spices to find out why.

“We know that the virus can

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DeepMind’s latest AI breakthrough can accurately predict the way proteins fold

Alphabet-owned DeepMind may be best known for building the AI that beat a world-class Go player, but the company announced another, perhaps more vital breakthrough this morning. As part of its work for the 14th Critical Assessment of Protein Structure Prediction, or CASP, DeepMind’s AlphaFold 2 AI has shown it can guess how certain proteins will fold themselves with surprising accuracy. In some cases, the results were perceived to be “competitive” with actual, experimental data.



diagram: AlphaFold 2


AlphaFold 2

“We have been stuck on this one problem – how do proteins fold up – for nearly 50 years,” said Professor John Moult, CASP chair and co-founder, in a DeepMind blog post. “To see DeepMind produce a solution for this, having worked personally on this problem for so long and after so many stops and starts, wondering if we’d ever get there, is a very special moment.”

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Researchers and enthusiasts across

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Study suggests mechanical properties of spike proteins can predict infectivity and lethality of different coronaviruses — ScienceDaily

When someone struggles to open a lock with a key that doesn’t quite seem to work, sometimes jiggling the key a bit will help. Now, new research from MIT suggests that coronaviruses, including the one that causes Covid-19, may use a similar method to trick cells into letting the viruses inside. The findings could be useful for determining how dangerous different strains or mutations of coronaviruses may be, and might point to a new approach for developing treatments.

Studies of how spike proteins, which give coronaviruses their distinct crown-like appearance, interact with human cells typically involve biochemical mechanisms, but for this study the researchers took a different approach. Using atomistic simulations, they looked at the mechanical aspects of how the spike proteins move, change shape, and vibrate. The results indicate that these vibrational motions could account for a strategy that coronaviruses use, which can trick a locking mechanism on the

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Shutting down COVID-19 virus’ destructive proteins with aerosolized molecules — ScienceDaily

Researchers at Georgetown University Medical Center have successfully used molecules made up of small strands of RNA to shut down the production of destructive proteins generated by the COVID-19 virus. Additionally, the researchers are working to aerosolize the RNA molecules so that they could be incorporated in an inhalable drug that would mitigate viral chaos. The finding appears online today in Gene Therapy.

A key to the Georgetown research efforts was the use of either microRNA (miRNA) or silencing RNA (siRNA, also known as small interfering RNA), both of which are RNA molecules. These molecules can guide the ultimate expression of how protein production occurs in a virus. And it is the proteins produced by SARS-CoV-2 (the virus that causes COVID-19) that wreak havoc in people.

SARS-CoV-2 bears biological similarities to other respiratory viruses, such as the seasonal flu. The use of Tamiflu® (oseltamivir) to treat and prevent infection

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Atom-scale models could help refine established theories on how proteins interact with solutions — ScienceDaily

It’s a long-standing assumption that the presence of water influences how proteins fold. A new study is challenging the details.

A paper in the American Chemical Society’s Journal of Physical Chemistry Letters shows proteins that presumably evolved to avoid water as they fold may actually behave in ways scientists did not anticipate.

That discovery could change how scientists think about hydrophobic (water-avoiding) and hydrophilic (water-attracting) interactions in solutions, according to a Rice University engineer.

Collaborators from Rice and Tulane universities and the Johns Hopkins University School of Medicine created atom-level models of polypeptides that showed folding is also influenced by thermal expansion of the solvents they occupy, but not in ways that match previous assumptions.

The long-held view is that hydrophobic amino acids, which avoid water by coming together as efficiently as possible, are a dominant force in protein folding, said Dilip Asthagiri, an associate research professor of chemical and

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Genetic eraser: Newly developed technology precisely and rapidly degrades targeted proteins

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IMAGE: A degron-fused protein of interest is recognized for rapid degradation by a TIR1 mutant only in the presence of an auxin analog, which initiates the degradation process. The target protein…
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Credit: Masato Kanemaki

Researchers can now more accurately and precisely target specific proteins in yeast, mammalian cells and mice to study how knocking down specific protein traits can influence physical manifestation in a cell or organism.

The Japan-based team published their results on November 11th in Nature Communications.

“Conditional gene knockout and small interfering RNA (siRNA), which is used to silence proteins without knocking them out completely, has been employed in many studies,” said Masato T. Kanemaki, professor at the National Institute of Genetics in the Research Organization of Information and Systems (ROIS). “However, these technologies are not ideal for studying highly dynamic processes, such as cell cycle, differentiation, or neural activity, because of the slow

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Sugar-coated viral proteins hijack and hitch a ride out of cells — ScienceDaily

Researchers from the Universities of Melbourne, York, Warwick and Oxford have shed light on how encapsulated viruses like hepatitis B, dengue and SARS-CoV-2 hijack the protein manufacturing and distribution pathways in the cell — they have also identified a potential broad spectrum anti-viral drug target to stop them in their tracks.

The findings have been published in PNAS today and are important to efforts to develop broad-spectrum antiviral agents.

Professor Spencer Williams from the School of Chemistry at Bio21 said the research will help define a new ‘host-directed’ approach for treating infections by encapsulated viruses.

“One approach to treating viral infections is to make a new drug for each virus that comes along. But it is slow. An alternative and attractive approach is to make a drug against a human target that viruses need to replicate. The same drug can then be used and reused against many different viruses, even

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Microscopy breakthrough reveals how proteins behave in 3-D

Microscopy breakthrough reveals how proteins behave in 3D
A new microscopy system that can can image individual molecules in 3D and capture the way they “wobble” uses a specially engineered glass plate developed by University of Rochester optical scientists. Credit: University of Rochester photo / J. Adam Fenster

Six years ago, the Nobel Prize in chemistry was awarded to three scientists for finding ways to visualize the pathways of individual molecules inside living cells.


Now, researchers at the University of Rochester and the Fresnel Institute in France have found a way to visualize those molecules in even greater detail, showing their position and orientation in 3-D, and even how they wobble and oscillate. The work could shed invaluable insights into the biological processes involved, for example, when a cell and the proteins that regulate its functions react to the virus that causes COVID-19.

“When a protein changes shape, it exposes other atoms that enhance the biological process, so

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Delivering proteins to testes could someday treat male infertility — ScienceDaily

According to the Mayo Clinic, about 15% of couples are infertile, and male infertility plays a role in over one-third of these cases. Often, problems with sperm development are to blame. Now, researchers reporting in ACS Nano have found a way to deliver a protein important for sperm cell production directly to mouse testicles, where it restored normal sperm development and allowed previously infertile mice to father pups.

Male infertility often happens because of a lack of sperm in the semen, which can result from damage to the blood-testis barrier (BTB). This barrier protects reproductive cells from harmful toxicants and drugs, and a protein called PIN1 is important for its function. Mice genetically engineered to lack PIN1 are infertile, with small testes, depleted sperm stem cells and a low sperm count. Although scientists have considered gene therapies to treat male infertility, these procedures are risky because they could cause unwanted

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