First recent US case of human bird flu confirmed in Colorado

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Turkeys stand in a barn on turkey farm near Manson, Iowa on Aug. 10, 2015. A Colorado prison inmate has tested positive for bird flu in the first confirmed case of a human being infected with the disease that has resulted in the death of millions of chickens and turkeys. The U.S. Centers for Disease Control and Prevention said Thursday, April 28, 2022, that the man who tested positive had been in a pre-release program and was helping removing chickens from an infected farm. Credit: AP Photo/Charlie Neibergall, File

A Colorado prison inmate has become the first person in the U.S. to test positive for bird flu in a recent outbreak that has led to the deaths of millions of chickens and turkeys, but federal officials say they still see little threat to the general public.

The U.S. Centers for Disease Control and Prevention said Thursday evening that the infected man had been in a prerelease program and was helping to remove chickens from an infected farm. The man, who was under age 40, reported fatigue for a few days but has recovered, state health and CDC officials said in a statement.

The man was isolated and is being treated with an antiviral drug. Other people involved in the bird removal operation in Colorado have tested negative, but they are being retested out of an abundance of caution.

The man was part of a crew of inmates nearing release who had been working at the farm before a case of was confirmed there on April 19, said Lisa Wiley, a spokeswoman for the Colorado Department of Corrections. When bird flu was detected at the farm in Montrose County, the inmates were asked to help kill and remove the birds.

Agriculture officials have reported an outbreak at one Montrose County farm with 58,000 broiler breeder chickens.

Despite the , the CDC considers the threat to the to be low because spread of the virus to people requires close contact with an infected bird.

Signals that could raise the might include multiple reports of virus infections in people from exposure to birds, or identification of spread from one person to another. The CDC also is monitoring for genetic changes to the H5N1 bird flu virus that is currently circulating. Any genetic changes could indicate the virus is adapting to spread more readily from birds to people or other mammals.

Many different bird flu viruses have infected humans worldwide since at least the 1990s, but health officials still say human infection is uncommon.

In 2002, H7N2 caused pinkeye and mild respiratory symptoms in people in the U.K. and the U.S. Four U.S. infections have been identified since 2002; two were transmitted from cats to humans in 2016.

More than 1,500 people in China have been infected with the H7N9 strain, largely in outbreaks between 2013 and 2017. This version caused serious infections among people and 40% of those who were hospitalized died.

A different variant of H5N1 has also circulated since 1997, infecting more than 880 people, and it had a 50% case fatality rate.

The current H5N1 variant has been spreading among backyard and commercial chicken and turkey flocks in the U.S. since late February. Viruses have been found in U.S. commercial and backyard birds in 29 states and in wild birds in 34 states. More than 35 million chickens and turkeys have been killed and removed to avoid spread, the U.S. Department of Agriculture reported.

The CDC said it has tracked the health of more than 2,500 people who have been exposed to H5N1-infected birds but that the inmate’s illness was the only confirmed case to date.

The agency said it was possible the man only had the present in his nose and that his body was not infected. Colorado public health officials say repeat testing on the man was negative for influenza. A nasal swab positive test result meets the agency’s criteria for considering it an infection.

“The appropriate public health response at this time is to assume this is an infection and take actions to contain and treat,” the CDC statement said.



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First recent US case of human bird flu confirmed in Colorado (2022, April 29)
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New research recommends multinational ocean sanctuaries to help corals survive climate change

Marine scientists studying coral responses in the field at Papua, New Guinea. Credit: Tom Shlesinger

With the growing severity of marine heatwaves, mass coral bleaching and mortality have become widespread. A new study led by researchers at Florida Tech recommends multinational networks of protected reefs as the best chance corals have to persist through climate change.

The research was led by Rob van Woesik, professor and director of the Institute for Global Ecology, and post-doctoral fellow Tom Shlesinger, both from Florida Tech, and 26 colleagues from around the world. It was published recently in Global Change Biology.

One of the greatest challenges for science is to combine findings across multiple disciplines and make useful recommendations for conservation. In their paper, van Woesik and colleagues summarize recent coral-bleaching discoveries, evaluate which data and processes can improve predictive models, and provide information to guide conservation efforts.

“While traditional marine reserves were commonly designed to prevent over-harvesting, the study recommends the establishment of networks of huge ‘mesoscale’ multinational sanctuaries to preserve the genetic diversity necessary to fuel evolutionary adaptation,” van Woesik said. “To ‘climate-proof’ reefs, we need to conserve both and .”

“There are several examples of such large multi-national networks of protected areas on land, and we need to make similar efforts in the ocean,” Florida Tech’s Shlesinger said.

Climate change threatens coral reefs by causing heat stress events that lead to widespread coral bleaching and mortality. Yet, some species and reefs seem to do better and still thrive, like the ones seen here in Papua, New Guinea. Credit: Tom Shlesinger

The paper reports that recent studies have identified several areas of potential climate-change refuges, including northwestern Indonesia, the central Philippines, Malaysia, French Polynesia, the northern Red Sea, Hawaii, Cuba and the Bahamas.

The study also suggests increasing in-country conservation efforts but also linking those efforts across national boundaries, Shlesinger noted.

“Focusing on critical biological processes and scaling those from the through the individual and population levels and up to the reef as a whole will be key to improve not only our current understanding but also our predictive capabilities,” van Woesik said.

He added, “Innovative, interdisciplinary solutions and novel molecular methods will help resolve responses to thermal stress and, therefore, can improve the identification of corals best suited for .”

Despite the global decline trajectory of coral reefs and mass bleaching and mortality events caused by marine heatwaves, some coral reefs and species are more resistant and resilient, like the ones depicted in this photo from the Gulf of Aqaba in the Middle East. Credit: Tom Shlesinger

The best way to support the resilience, adaptation and recovery of coral reefs is of course to urgently reduce global emissions of greenhouse gases, the authors suggest, while also working cooperatively to create both local and mesoscale coral-reef sanctuaries.

“Alongside the urgent global need to reduce emissions of greenhouse gases, all possible local and multinational actions should be made to conserve —one of the most wondrous ecosystems on the planet—into the future,” the authors write.

The article, “Coral-bleaching responses to across biological scales,” is available at Global Change Biology.



More information:
Robert Woesik et al, Coral‐bleaching responses to climate change across biological scales, Global Change Biology (2022). DOI: 10.1111/gcb.16192

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New research recommends multinational ocean sanctuaries to help corals survive climate change (2022, April 29)
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New technique shows in detail where drug molecules hit their targets in the body

A team at Scripps Research invented a new method, called CATCH, that shows how drugs hit their targets in the body. Cells targeted by a drug (pargyline shown in cyan) can be identified by multiple rounds of immunolabeling (red showing neurons; yellow showing dopaminergic/noradrenergic neurons; blue showing cell nuclei). Credit: Scripps Research

Scientists at Scripps Research have invented a way to image, across different tissues and with higher precision than ever before, where drugs bind to their targets in the body. The new method could become a routine tool in drug development.

Described in a paper in Cell on April 27, 2022, the new method, called CATCH, attaches fluorescent tags to molecules and uses chemical techniques to improve the fluorescent signal. The researchers demonstrated the method with several different experimental drugs, revealing where—even within —the drug molecules hit their targets.

“This method ultimately should allow us, for the first time, to see relatively easily why one drug is more potent than another, or why one has a particular side effect while another one doesn’t,” says study senior author Li Ye, Ph.D., assistant professor of neuroscience at Scripps Research and The Abide-Vividion Chair in Chemistry and Chemical Biology.

The study’s first author, Zhengyuan Pang, is a graduate student in the Ye lab. The study also was a close collaboration with the laboratory of Ben Cravatt, Ph.D., Gilula Chair of Chemical Biology at Scripps Research.

“The unique environment at Scripps Research, where biologists routinely work together with chemists, is what made the development of this technique possible,” Ye says.

Understanding where drug molecules bind their targets to exert their —and side effects—is a basic part of . However, drug-target interaction studies traditionally have involved relatively imprecise methods, such as bulk analyses of drug-molecule concentration in entire organs.

The CATCH method involves the insertion of tiny chemical handles into drug molecules. These distinct chemical handles don’t react with anything else in the body, but do allow the addition of fluorescent tags after the have bound to their targets. In part because human or animal tissue tends to diffuse and block the light from these fluorescent tags, Ye and his team combined the tagging process with a technique that makes tissue relatively transparent.

In this initial study, the researchers optimized and evaluated their method for “covalent drugs,” which bind irreversibly to their targets with stable chemical bonds known as covalent bonds. This irreversibility of binding makes it particularly important to verify that such drugs are hitting their intended targets.

The scientists first evaluated several covalent inhibitors of an enzyme in the brain called fatty acid amide hydrolase (FAAH). FAAH inhibitors have the effect of boosting levels of cannabinoid molecules, including the “bliss molecule” anandamide, and are being investigated as treatments for pain and mood disorders. The scientists were able to image, at the single-cell level, where these inhibitors hit their targets within large volumes of mouse brain tissue, and could easily distinguish their different patterns of target engagement.

In one experiment, they showed that an experimental FAAH inhibitor called BIA-10-2474, which caused one death and several injuries in a clinical trial in France in 2016, engages unknown targets in the midbrain of mice even when the mice lack the FAAH enzyme—offering a clue to the source of the inhibitor’s toxicity.

In other tests demonstrating the unprecedented precision and versatility of the new method, the scientists showed that they could combine drug-target imaging with separate fluorescent-tagging methods to reveal the cell types to which a drug binds. They also could distinguish drug-target engagement sites in different parts of neurons. Finally, they could see how modestly different doses of a drug often strikingly affect the degree of target engagement in different brain areas.

The proof-of-principle study is just the beginning, Ye emphasizes. He and his team plan to develop CATCH further for use on thicker tissue samples, ultimately perhaps whole mice. Additionally, they plan to extend the basic approach to more common, non-covalently-binding drugs and chemical probes. On the whole, Ye says, he envisions the new method as a basic tool not only for drug discovery but even for basic biology.

“In situ Identification of Cellular Drug Targets in Mammalian Tissue” was co-authored by Zhengyuan Pang, Michael Schafroth, Daisuke Ogasawara, Yu Wang, Victoria Nudell, Neeraj Lal, Dong Yang, Kristina Wang, Dylan Herbst, Jacquelyn Ha, Carlos Guijas, Jacqueline Blankman, Benjamin Cravatt and Li Ye—all of Scripps Research during the study.



More information:
Zhengyuan Pang et al, In situ identification of cellular drug targets in mammalian tissue, Cell (2022). DOI: 10.1016/j.cell.2022.03.040

Journal information:
Cell



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Discovery of aberrant protein that kills bacterial cells could help unravel mechanism of certain antibiotics

Light microscope images of E. coli cells in transmitted light (left) and reflected light that picks up the red fluorescence of a dye staining the cells’ DNA (right). In normal cells (upper panel), the DNA is spread throughout the cells. But in cells expressing the aberrant plant protein identified in this study (bottom panel) all the DNA within each cell has collapsed into a dense mass. DNA condensation also occurs after bacteria have been treated with aminoglycoside antibiotics. Credit: Brookhaven National Laboratory

Biologists at the U.S. Department of Energy’s Brookhaven National Laboratory and their collaborators have discovered an aberrant protein that’s deadly to bacteria. In a paper just published in the journal PLOS ONE, the scientists describe how this erroneously built protein mimics the action of aminoglycosides, a class of antibiotics. The newly discovered protein could serve as a model to help scientists unravel details of those drugs’ lethal effects on bacteria—and potentially point the way to future antibiotics.

“Identifying new targets in bacteria and alternative strategies to control is going to become increasingly important,” said Brookhaven biologist Paul Freimuth, who led the research. Bacteria have been developing resistance to many commonly used drugs, and many scientists and doctors have been concerned about the potential for large-scale outbreaks triggered by these , he explained.

“What we’ve discovered is a long way from becoming a drug, but the first step is to understand the mechanism,” Freimuth said. “We’ve identified a single that mimics the effect of a complex mixture of aberrant proteins made when bacteria are treated with aminoglycosides. That gives us a way to study the mechanism that kills the bacterial . Then maybe a new family of inhibitors could be developed to do the same thing.”

Following an interesting branch

The Brookhaven scientists, who normally focus on energy-related research, weren’t thinking about human health when they began this project. They were using E. coli bacteria to study genes involved in building plant cell walls. That research could help scientists learn how to convert (biomass) into biofuels more efficiently.

But when they turned on expression of one particular plant gene, enabling the bacteria to make the protein, the cells stopped growing immediately.

“This protein had an acutely toxic effect on the cells. All the cells died within minutes of turning on expression of this gene,” Freimuth said.

Understanding the basis for this rapid inhibition of cell growth made an ideal research project for summer interns working in Freimuth’s lab.

“Interns could run experiments and see the effects within a single day,” he said. And maybe they could help figure out why a plant protein would cause such dramatic damage.

Brookhaven Lab biologist Paul Freimuth and co-author Feiyue Teng, a scientist in Brookhaven Lab’s Center for Functional Nanomaterials (CFN), at the light microscope used to image bacteria in this study. Credit: Brookhaven National Laboratory

Misread code, unfolded proteins

“That’s when it really started to get interesting,” Freimuth said.

The group discovered that the toxic factor wasn’t a plant protein at all. It was a strand of amino acids, the building blocks of proteins, that made no sense.

This nonsense strand had been churned out by mistake when the bacteria’s ribosomes (the cells’ protein-making machinery) translated the letters that make up the “out of phase.” Instead of reading the code in chunks of three letters that code for a particular amino acid, the ribosome read only the second two letters of one chunk plus the first letter of the next triplet. That resulted in putting the wrong amino acids in place.

“It would be like reading a sentence starting at the middle of each word and joining it to the first half of the next word to produce a string of gibberish,” Freimuth said.

The gibberish protein reminded Freimuth of a class of antibiotics called aminoglycosides. These antibiotics force ribosomes to make similar “phasing” mistakes and other sorts of errors when building proteins. The result: all the bacteria’s ribosomes make gibberish proteins.

“If a bacterial cell has 50,000 ribosomes, each one churning out a different aberrant protein, does the toxic effect result from one specific aberrant protein or from a combination of many? This question emerged decades ago and had never been resolved,” Freimuth said.

The new research shows that just a single aberrant protein can be sufficient for the .

That wouldn’t be too farfetched. Nonsense strands of amino acids can’t fold up properly to become fully functional. Although misfolded proteins get produced in all cells by chance errors, they usually are detected and eliminated completely by “” machinery in healthy cells. Breakdown of quality control systems could make aberrant proteins accumulate, causing disease.

Messed-up quality control

The next step was to find out if the aberrant plant protein could activate the bacterial cells’ quality control system—or somehow block that system from working.

Freimuth and his team found that the aberrant plant protein indeed activated the initial step in protein quality control, but that later stages of the process directly required for degradation of aberrant proteins were blocked. They also discovered that the difference between cell life and death was dependent on the rate at which the aberrant protein was produced.

“When cells contained many copies of the gene coding for the aberrant plant protein, the quality control machinery detected the protein but was unable to fully degrade it,” Freimuth said. “When we reduced the number of gene copies, however, the quality control machinery was able to eliminate the toxic protein and the cells survived.”

The same thing happens, he noted, in cells treated with sublethal doses of aminoglycoside antibiotics. “The quality control response was strongly activated, but the cells still were able to continue to grow,” he said.

Model for mechanism

These experiments indicated that the single aberrant plant protein killed cells by the same mechanism as the complex mixture of aberrant proteins induced by aminoglycoside antibiotics. But the precise mechanism of cell death is still a mystery.

“The good news is that now we have a single protein, with a known amino acid sequence, that we can use as a model to explore that mechanism,” Freimuth said.

Scientists know that cells treated with the antibiotics become leaky, allowing things like salts to seep in at toxic levels. One hypothesis is that the misfolded proteins might form new channels in cellular membranes, or alternatively jam open the gates of existing channels, allowing diffusion of salts and other toxic substances across the cell membrane.

“A next step would be to determine structures of our protein in complex with membrane channels, to investigate how the protein might inhibit normal channel function,” Freimuth said.

That would help advance understanding of how the aberrant proteins induced by aminoglycoside antibiotics kill —and could inform the design of new drugs to trigger the same or similar effects.



More information:
A polypeptide model for toxic aberrant proteins induced by aminoglycoside antibiotics, PLoS ONE (2022). DOI: 10.1371/journal.pone.0258794

Citation:
Discovery of aberrant protein that kills bacterial cells could help unravel mechanism of certain antibiotics (2022, April 29)
retrieved 30 April 2022
from https://phys.org/news/2022-04-discovery-aberrant-protein-bacterial-cells.html

This document is subject to copyright. Apart from any fair dealing for the purpose of private study or research, no
part may be reproduced without the written permission. The content is provided for information purposes only.

% %item_read_more_button%% Hexbyte Glen Cove Educational Blog Repost With Backlinks — #metaverse #vr #ar #wordpress