(Family Features) Even though cooler days may seem far off, now is the best time to plan ahead for a healthy winter. One common respiratory illness, respiratory syncytial virus, or RSV, usually causes mild, cold-like symptoms, but it can be severe and even deadly for older people.

“As we grow older, our immune systems do not work as well and we are more likely to have chronic conditions, which means we are at increased risk of getting very sick from common viruses as we age,” said Alison Barkoff, who leads the Administration for Community Living within the U.S. Department of Health and Human Services. “Getting vaccinated is the best protection against fall respiratory viruses like RSV. It can help keep symptoms mild and help keep people out of the hospital.”

Here’s what older Americans need to know about RSV and vaccines this fall, according to the Risk Less. Do More. Public Education Campaign.

Prevention is key. The Centers for Disease Control and Prevention recommends that everyone 75 years and older get an RSV vaccine. Also, people between 60-74 should get vaccinated if they have conditions such as heart or lung disease, diabetes, obesity or a weakened immune system. The vaccine cuts the risk of hospitalization from RSV by at least half.

People living in nursing homes, assisted living or other long-term care facilities are at even higher risk. There are many people living together in these facilities who have medical conditions that make them more likely to get very sick. While vaccines may not always stop infection, they can prevent severe illness. So, vaccination is very important for residents of long-term care facilities.

RSV vaccines are available. Three RSV vaccines have been approved for older adults by the U.S. Food and Drug Administration. You only need a single dose that you can get at any time of the year, but getting the vaccine in the early fall offers the best protection for the late fall and winter, when RSV usually peaks. Getting the vaccine early gives your immune system enough time to build up protection.

RSV vaccines are the best protection. The RSV vaccines have gone through extensive testing. Last year, more than 20 million older adults were vaccinated safely. Mild side effects, such as pain, redness or swelling at the injection site sometimes happen, but they usually go away on their own in a few days. Serious allergic reactions from RSV vaccines are rare.

Prevention is the best option. Respiratory virus vaccines, including RSV vaccines, can help protect older adults from serious illness.

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Talk to your doctor and visit cdc.gov/RSV to learn more.

Photo courtesy of Shutterstock

SOURCE:
United States Department of Health and Human Services

Our Lifestyle section on STM Daily News is a hub of inspiration and practical information, offering a range of articles that touch on various aspects of daily life. From tips on family finances to guides for maintaining health and wellness, we strive to empower our readers with knowledge and resources to enhance their lifestyles. Whether you’re seeking outdoor activity ideas, fashion trends, or travel recommendations, our lifestyle section has got you covered. Visit us today at https://stmdailynews.com/category/lifestyle/ and embark on a journey of discovery and self-improvement.

Research pinpoints key to the cold sore virus’s ability to evade treatment, offering broader clues on antiviral drug resistance

Newswise — All organisms — from fungi to mammals — have the capacity to evolve and adapt to their environments. But viruses are master shapeshifters with an ability to mutate greater than any other organism. As a result, they can evade treatments or acquire resistance to once-effective antiviral medications.

Is the Herpes Simplex Virus Becoming Impervious to Drugs?

Working with herpes simplex virus (HSV), a new study led by Harvard Medical School researchers sheds light on one of the ways in which the virus becomes resistant to treatment, a problem that could be particularly challenging among people with compromised immune function, including those receiving immune-suppressive treatment and those born with immune deficiencies.

Using a sophisticated imaging technique called cryogenic electron microscopy (cryo-EM), the researchers found that how parts of a protein responsible for viral replication move into different positions can alter the virus’s susceptibility to medicines.

The findings, published Aug. 27 in Cell, answer long-standing questions about why certain viruses, but not others, are susceptible to antiviral medications and how viruses become impervious to drugs. The results could inform new approaches that impede viruses’ capacity to outpace effective therapies.

Counterintuitive results

Researchers have long known changes that occur on the parts of a virus where antiviral drugs bind to it can render it resistant to therapy. However, the HMS researchers found that, much to their surprise, this was often not the case with HSV.

Instead, the investigators discovered that protein mutations linked to drug resistance often arise far from the drug’s target location. These mutations involve alterations that change the movements of a viral protein, or enzyme, that allows the virus to replicate itself. This raises the possibility that using drugs to block or freeze the conformational changes of these viral proteins could be a successful strategy for overcoming drug resistance.

“Our findings show that we have to think beyond targeting the typical drug-binding sites,” said the study’s senior author, Jonathan Abraham, associate professor of microbiology in the Blavatnik Institute at HMS and infectious disease specialist at Brigham and Women’s Hospital. “This really helps us see drug resistance in a new light.”

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The new findings propel the understanding of how alterations in the conformation of a viral protein — or changes in how the different parts within that protein move when it carries out its function — fuel drug resistance and may be relevant for understanding drug effectiveness and drug resistance in other viruses, the researchers noted.

HSV, estimated to affect billions of people worldwide, is most commonly known as the cause of cold sores and fever blisters, but it can also lead to serious eye infections, brain inflammation, and liver damage in people with compromised immunity. Additionally, HSV can be transmitted from mother to baby via the birth canal during delivery and cause life-threatening neonatal infections. 

Clues on resistance rooted in structure and movement

A virus can’t replicate on its own. To do so, viruses must enter a host cell, where they unleash their replication tools — proteins called polymerases — to make copies of themselves.

The current study focused on one such protein — a viral DNA polymerase — crucial for HSV’s ability to reproduce and propagate itself. The ability to carry out its function is rooted in the DNA polymerase’s structure, often likened to a hand with three parts: the palm, the thumb, and the fingers, each carrying out critical functions.

Given their role in enabling replication, these polymerases are critical targets of antiviral drugs, which aim to stop the virus from reproducing itself and halt the spread of infection. The HSV polymerase is the target of acyclovir, the leading antiviral drug for treating HSV infection, and of foscarnet, a second-line drug used for drug-resistant infections. Both drugs work by targeting the viral polymerase but do so in different ways.

Scientists have long struggled to fully understand how alterations in the polymerase render the virus impervious to normal doses of antiviral drugs and, more broadly, why acyclovir and foscarnet are not always effective against the altered forms of the HSV polymerase.

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“Over the years, the structures of many polymerases from various organisms have been determined, but we still don’t fully understand what makes some polymerases, but not others, susceptible to certain drugs,” Abraham said. “Our study reveals that how the different parts of the polymerases move, known as their conformational dynamics, is a critical component of their relative susceptibility to drugs.” 

Proteins, including polymerases, are not rigid, motionless objects. Instead, they are flexible and dynamic.Composed of amino acids, they initially fold into a steady, three‐dimensional shape known as the native conformation — their baseline structure. But as a result of various bonding and dispersing forces, the different parts of proteins can move when they come into contact with other cellular components as well as through external influences, such as changes in pH or temperature. For example, the fingers of a polymerase protein can open and close, as would the fingers of a hand.

Conformational dynamics — the ability of different parts of a protein to move — allow them to efficiently administer many essential functions with a limited number of ingredients. A better understanding of polymerase conformational dynamics is the missing link between structures and functions, including whether a protein responds to a drug and whether it could become resistant to it down the road.

Unraveling the mystery

Many structural studies have captured DNA polymerases in various distinct conformations. However, a detailed understanding of the impact of polymerase conformational dynamics on drug resistance is lacking. To solve the puzzle, the researchers carried out a series of experiments, focusing on two common polymerase conformations — an open one and a closed one — to determine how each affects drug susceptibility.

First, using cryo-EM, they conducted structural analysis to get high-resolution visualizations of the atomic structures of HSV polymerase in multiple conformations, as well as when bound to the antiviral drugs acyclovir and foscarnet. The drug-bound structures revealed how the two drugs selectively bind polymerases that more readily adopt one conformation versus another. One of the drugs, foscarnet, works by trapping the fingers of the DNA polymerase so that they are stuck in a so-called closed configuration.

Further, structural analysis paired with computational simulations suggested that several mutations that are distant from the sites of drug binding confer antiviral resistance by altering the position of the polymerase fingers responsible for closing onto the drug to halt DNA replication.

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The finding was an unexpected twist. Up until now, scientists have believed that polymerases closed partially only when they attached to DNA and closed fully only when they added a DNA building block, a deoxynucleotide. It turns out, however, that HSV polymerase can fully close just by being near DNA. This makes it easier for acyclovir and foscarnet to latch on and stop the polymerase from working, thus halting viral replication.

“I’ve worked on HSV polymerase and acyclovir resistance for 45 years. Back then I thought that resistance mutations would help us understand how the polymerase recognizes features of the natural molecules that the drugs mimic,” said study co-author Donald Coen, professor of biological chemistry and molecular pharmacology at HMS. “I’m delighted that this work shows that I was wrong and finally gives us at least one clear reason why HSV polymerase is selectively inhibited by the drug.”

Authorship, funding, disclosures

Additional authors included Sundaresh Shankar, Junhua Pan, Pan Yang, Yuemin Bian, Gábor Oroszlán, Zishuo Yu, Purba Mukherjee, David J. Filman, James M. Hogle, Mrinal Shekhar.

This work was supported by the National Institutes of Health (awards R21 AI141940 and R01 AI19838), with additional funding from a Centers for Integrated Solutions in Infectious Diseases grant.

What Enables Herpes Simplex Virus To Become Impervious to Drugs?

Source: Harvard Medical School

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(Family Features) Protecting students as they travel to and from school takes many forms. Parents and educators alike teach kids to be mindful of traffic and responsible while riding and waiting at the bus stop. Drivers are trained to avoid accidents to safeguard the children in their care. Another way to protect kids traveling to and from school involves the mode of transportation they use.

According to the National Transportation Safety Board, 25 million children across the country ride to school every day in nearly 500,000 school buses. Yet the way kids ride to school today is very much the way children rode to school 25 years ago, in an aging diesel school bus. These buses are not only expensive to operate, they also pose potential harm to children’s health, the community and the environment.

While there are diverse energy options that can achieve cleaner, healthier school transportation, propane is an environmentally friendly and affordable energy source.

“With significant investments being made to clean up the nation’s school bus fleet, such as the Environmental Protection Agency’s Clean School Bus Program, there’s never been a better time to prioritize clean transportation,” said Tucker Perkins, president and CEO for the Propane Education & Research Council. “Affordable and available solutions, like propane, should be implemented immediately to move further down the path to zero emissions and decarbonize our nation’s school bus fleets.”

At BetterOurBuses.com you can learn how to open dialogue with your school district about clean transportation by sharing the benefits of propane school buses, including:

Student Health

Propane buses are better for children’s health compared to diesel buses because they reduce harmful pollutants. The cloud of black smoke that comes from the tailpipe of a diesel bus contains harmful emissions like nitrogen oxide and particulate matter. Propane buses eliminate that issue, reducing harmful nitrogen oxide emissions by up to 96% compared to diesel and emitting near-zero particulate matter emissions.

Beyond the implications for asthma, bronchitis and other respiratory problems, propane school buses provide a quieter ride than diesel buses, which means those driving children to school are better equipped to hear potential concerns and protect riders’ safety.

The Environment

Propane reduces harmful emissions that impact student health, the environment and air quality in the community. It is a low-carbon energy source that can accelerate decarbonization of the nation’s school bus fleet. It is also non-toxic to groundwater and soil. Both propane and electric vehicles can reduce emissions compared to diesel, but propane does it at a fraction of the cost. School districts can buy three propane buses for the cost of one electric bus, allowing them to retire aging diesel buses three times faster by choosing propane.

Cost Savings

Propane school buses are an affordable option for school districts. The operating cost of propane school buses are half the cost of diesel, allowing school districts to put more money back into the classroom. If all the diesel buses in the U.S. were converted to operate on propane, enough money could be saved to hire 23,000 teachers.

Reliability

Propane has a range of 400 miles, which makes it a good choice for vehicles like school buses, which need to travel long distances without stopping to recharge or refuel, providing a reliable ride for students. Propane school buses also have the power and performance to travel in all kinds of weather and across all types of terrain while diesel and electric buses can be impacted by freezing weather.

SOURCE:
Propane Education & Research Council

Our Lifestyle section on STM Daily News is a hub of inspiration and practical information, offering a range of articles that touch on various aspects of daily life. From tips on family finances to guides for maintaining health and wellness, we strive to empower our readers with knowledge and resources to enhance their lifestyles. Whether you’re seeking outdoor activity ideas, fashion trends, or travel recommendations, our lifestyle section has got you covered. Visit us today at https://stmdailynews.com/category/lifestyle/ and embark on a journey of discovery and self-improvement.

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