Category Archives: Biochemistry

March: STEM BME event | News and features – University of Bristol

Last month, BME pupils from City Academy in Bristol got their first taste of Science, Technology, Engineering and Maths (STEM) thanks to black students and professionals from the Schools of Biochemistry, Chemistry, Mathematics and CAME Engineering.

Aiming to encourage black pupils from City Academy to come to University, and to consider wider careers in STEM subjects, the event showcased the roles of black engineers and scientists and was inspired by discussions with the Assistant Principal for Inclusion at City Academy in Bristol Aisha Thomas. In a 2018 study, Aisha found that there are 26 black working teachers in Bristol's secondary schools, out of more than 1,300 across the city and found that this lack of representation is one of the factors that leads to low inclusion of black students in Higher Education.

Thirty-one pupils from City Academy attended the event, listening to talks from Professor Tanniemola Liverpool (Mathematics, University of Bristol) and Benjamin Omasanuwa (Head of Mechanical Engineering Design Office, Safran Seats GB).

The pupils also took part in demonstrations including practical sessions on forensic science, ink-jet printing and a demonstration of a Chaotic pendulum by Mictroy Mitchell. Mictroy was born in Kingston, Jamaica, but when he came to the UK, he went to City Academy. After working in the railway engineering sector, he moved to the University of Bristol as a Research Technician in the Earthquake Laboratory.

Mictroy said: "I love giving back to the community. It fills my soul with joy knowing that I am helping and inspiring the younger generation."

The event was set up by Lara Lalemi, a Chemistry student who last year organised the Being BME in STEM workshop and report, which highlighted the need for work around the inclusion of minority groups.

Lara said: "In the current climate, where there is a lack of domicile BME students studying a STEM subject, this event endeavoured to show the fun side of chemistry, biochemistry and engineering, encouraging young students to consider studying them in higher education. We want to inspire the next generation of scientists, mathematicians and engineers and this event is work towards that."

Professor Stephen Eichhorn, co-organiser of the event, said: "As a white-male Professor in the UK I represent the majority in my profession. It is important to recognise that barriers to access Higher Education, particularly in STEM subjects, are significant. This is especially true for black students and professionals.

"We need to increase opportunities and routes into Higher education. One size does not fit all. We also need to increase representation of black educators in Higher Education. If we don't do this, we miss out on great talent pools of potential."

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March: STEM BME event | News and features - University of Bristol

Automatic Veterinary Biochemistry Analyzer Market 2020 By Top Key Players/Manufacturers, Type and Application, Regions, Industry Analysis, Growth,…

The latest research report on the Automatic Veterinary Biochemistry Analyzer Market published by Verified Market Research provides a profound awareness of the various market dynamics such as Trends, drivers, challenges and opportunities. The report explains in more detail the micro and macroeconomic elements that are expected to influence the growth of the Automatic Veterinary Biochemistry Analyzer Market over the forecast period (2020-2026).

The Global Automatic Veterinary Biochemistry Analyzer Market is growing at a faster pace with substantial growth rates over the last few years and is estimated that the market will grow significantly in the forecasted period i.e. 2019 to 2026.

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U of T researchers hunt for antivirals to treat COVID-19 patients – News@UofT

Researchers from the University of Torontos Donnelly Centre for Cellular and Biomolecular Research are working on developingantivirals that can combat thenovel coronavirus outbreak.

Led bySachdev Sidhu, a professor of molecular genetics, the team will apply their protein engineering technology to identify promising therapeutics.

We have diverse expertise on our team from across U of T and the University of Manitoba, which is renowned for its virology research, and we have already demonstrated that we can engineer proteins that inhibit MERS, a related coronavirus, says Sidhu, who, in addition to the Donnelly Centre holds cross appointments in the Faculty of Medicine and at the Institute of Biomaterials and Biomedical Engineering. We will now expand on this work to design therapeutics for COVID-19.

The team recently received almost $900,000 over two years from the federal government through a rapid funding competition announced on Feb. 10 to address the COVID-19 outbreak.

Sidhu is collaborating withRoman Melnyk, a senior scientist at the Hospital for Sick Children and assistant professor of biochemistry at U of T, andBrian Mark, a structural virologist and professor at the University of Manitoba. In a 2016 proof-of-principle study withMarjolein Kikkert, a virologist at Leiden University in the Netherlands, they applied a protein engineering pipeline developed by Sidhus team to create proteins that inhibit a related coronavirus that caused the Middle East Respiratory Syndrome (MERS) outbreak in 2012.

Wei Zhang, then a post-doctoral researcher in Sidhus lab and now an assistant professor at the University of Guelph,received a national innovation award for this research.

The researchers now plan to use the same strategy to battle the coronavirus behind the COVID-19global health crisis, which the World Health Organization today declared a pandemic.

Since the outbreak began in China in late 2019, the virus has spread to every continentexcept Antarctica, with more than 120,000 confirmed cases and more than 4,000 deaths, according to the latest figures. And while researchers around the world are racing to develop a vaccine, that is only a part of the solution, Sidhu says.

Even if a vaccine becomes available, not everyone is going to get vaccinated, says Sidhu. We see that with the flu the vaccination rates are far from 100 per cent. Should the virus become endemic and end up circulating in the population like the flu, medicines that stop the virus from replicating in an already infected person will be as important as vaccines, which prevent infection, according to Sidhu.

Jacky Chung, a research associate in the Sidhu lab, will spearhead the project by first engineering proteins that can inhibit the virus. The team will then search for small molecules that behave in the same way since they are easier to develop into therapeutics than proteins.

It's important to get the therapeutic inside the cells, which is where the virus replicates, says Chung. And small molecules can get into cells much more readily than proteins, which are much larger.

At the heart of the approach lies a protein called ubiquitin, named for being present in all plant and animal cells. Ubiquitin is an essential part of the cellular machinery that the virus hijacks for its own benefit. Upon infection, the virus releases proteins that interfere with human ubiquitin and allow it to bypass the hosts defence system and spread in the body.

To block the virus, the researchers will create synthetic ubiquitin variants (UbV) that thwart rather than aid its ability to replicate. By analyzing the molecular structures of different UbVs bound to the viral protein, they will gain clues into the kinds of small molecules that are most likely to be effective against the virus.

Sidhu says that, within two years, they should have candidate molecules that could be developed into therapeutics. We know there are literally armies of medicinal chemists and various companies that could then optimize the molecule into a drug that can be given to humans, says Sidhu who was previously at pharmaceutical giant Genentech and has founded six startups since joining the university.

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U of T researchers hunt for antivirals to treat COVID-19 patients - News@UofT

‘Seeing the Invisible’ exhibit opens in the Chappell Family Gallery – Duke Chronicle

If youve walked through the Chappell Family gallery in Perkins Library any time recently, youve probably noticed it: the big colorful arrows and ribbons on the walls, the twisting wires and strange diagrams galore.

The exhibit, called Seeing the Invisible: 50 Years of Macromolecule Visualization, chronicles the development of a key visualization technique in the field of biology. With its grand opening this past Wednesday, Feb 23, the display is centered around the ever-important ribbon model for proteins. If youve taken biology classes, then you would surely recognize the model, widely used due to its ability to easily show the -Helice and -Strands in the secondary structure of protein molecules.

The exhibit, which replaces last semesters Senses of Venice, focuses on the work of Duke professors and married couple Jane and David Richardson, who pioneered the ribbon model often called the Richardson model, reflecting how significant their contribution is to the subject.

Jane Richardson, who graduated with a Bachelors degree in philosophy from Swarthmore College in 1962 before earning a Masters degree from Harvard in 1966, took a non-typical route toward science. But even though she may have not followed the traditional path for a biology researcher, her philosophy background was helpful and unique enough.

In a 2018 interview with the Chronicle, Jane said, [Philosophy] teaches you not just to do critical thinking, but really to push it and always question an assumption.

However, despite her heavy involvement in philosophy, Richardson had long been interested in science, winning the Westinghouse Science Talent Search in high school for calculating the orbit of the satellite Sputnik. When she joined her husband at an MIT lab, where David Richardson was working toward a doctoral degree, to study staphylococcal nuclease protein with X-ray crystallography, she began a career-long focus on protein structure.

The Richardsons then began trailblazing new frontiers within the discipline. After moving to Duke University in 1970, they found the first crystal structure of the enzyme superoxide dismutase. Without the current-day technology of synchrotrons, or strong sources of X-rays, scientists, including the Richardsons, relied on crystallography. In the following decade, they came up with the first ribbon drawings of the molecule, and by 1981, the first images of her famous ribbon model appeared in an article titled The anatomy and taxonomy of protein structure, published in the journal Advances in Protein Chemistry.

Creating this model, though, was not easy. It required years of research, and models were constructed in several different mediums, including the wire figures seen around the exhibit and even a wooden design created by a bevel miter saw (which was also used to build their home in the Duke forest). Most influential, though, would be the iconic dual drawings of the Staphylococcal nuclease. In the exhibit, there are both the primary sketch drawn by Jane Richardson and the final pen-and-ink version. She spent an entire year just learning to draw 2-D ribbon drawings that fully represented the entire 3-D protein molecule.

After their breakthrough with the ribbon model, the Richardsons continued to work and excel in the field of biochemistry. In 1985, Jane Richardson received the MacArthur Fellowship, and, even though she may not have completed a PhD degree program, she has been awarded three honorary doctorates over the years from Swarthmore College, the UNC Chapel Hill and the University of Richmond.

Even today, the couple keeps themselves busy. As the two heads of the Richardson lab here at Duke University, they oversee important research in the field of biochemistry. Questions about resolution and computer modeling remain pressing concerns in the Richardson Lab.

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'Seeing the Invisible' exhibit opens in the Chappell Family Gallery - Duke Chronicle

Biochemistry of Carbohydrates

Carbohydrates are carbon compounds that contain largequantities of hydroxyl groups. The simplest carbohydrates also contain eitheran aldehyde moiety (these are termed polyhydroxyaldehydes) or a ketone moiety (polyhydroxyketones). Allcarbohydrates can be classified as either monosaccharides, oligosaccharides or polysaccharides.Anywhere from two to ten monosaccharide units, linked by glycosidic bonds, make up an oligosaccharide.Polysaccharides are much larger, containing hundreds of monosaccharide units.The presence of the hydroxyl groups allows carbohydrates to interact with theaqueous environment and to participate in hydrogen bonding, both within andbetween chains. Derivatives of the carbohydrates can contain nitrogens,phosphates and sulfur compounds. Carbohydrates also can combine with lipid toform glycolipids or withprotein to form glycoproteins.

The predominant carbohydrates encountered in the bodyare structurally related to the aldotriose glyceraldehyde and to the ketotriose dihydroxyacetone. All carbohydratescontain at least one asymmetrical (chiral) carbon and are, therefore, opticallyactive. In addition, carbohydrates can exist in either of two conformations, asdetermined by the orientation of the hydroxyl group about the asymmetric carbonfarthest from the carbonyl. With a few exceptions, those carbohydrates that areof physiological significance exist in the D-conformation. The mirror-image conformations, called enantiomers, are in the L-conformation.

The monosaccharides commonly found in humans areclassified according to the number of carbons they contain in their backbonestructures. The major monosaccharides contain four to six carbon atoms.

The aldehyde and ketone moieties of the carbohydrateswith five and six carbons will spontaneously react with alcohol groups presentin neighboring carbons to produce intramolecular hemiacetals or hemiketals, respectively. This results in the formation of five-or six-membered rings. Because the five-membered ring structure resembles theorganic molecule furan, derivatives with this structure are termed furanoses. Those with six-membered rings resemble the organicmolecule pyran and are termed pyranoses

Such structures can be depicted byeither Fischer or Haworthstyle diagrams. The numbering of thecarbons in carbohydrates proceeds from the carbonyl carbon, for aldoses, or thecarbon nearest the carbonyl, for ketoses.

Structural models of glucose. Glucose can exist in the - and -enantiomeric forms in solution. The structure of either form of glucose is commonly depicted using cyclic Fischer projection or the cyclic Haworth projection.

The rings can open and re-close, allowing rotation tooccur about the carbon bearing the reactive carbonyl yielding two distinctconfigurations ( and ) of the hemiacetals and hemiketals. The carbon aboutwhich this rotation occurs is the anomeric carbon and the twoforms are termed anomers. Carbohydrates can change spontaneously between the and configurations: a process known asmutarotation. When drawn in the Fischer projection, the configuration places the hydroxyl attached to the anomeric carbon to the right,towards the ring. When drawn in the Haworth projection, the configuration places the hydroxyl downward.

The spatial relationships of the atoms of the furanose and pyranose ring structures are more correctly describedby the two conformations identified as the chair form and the boatform. The chair form is the more stable of the two. Constituents of thering that project above or below the plane of the ring are axial and those that project parallelto the plane are equatorial. In the chair conformation, the orientationof the hydroxyl group about the anomeric carbon of -D-glucose is axial and equatorial in -D-glucose.

Covalent bonds between the anomeric hydroxyl of acyclic sugar and the hydroxyl of a second sugar (or another alcohol containingcompound) are termed glycosidic bonds, and the resultant molecules are glycosides. The linkage of two monosaccharides to formdisaccharides involves a glycosidic bond. Several physiogically importantdisaccharides are sucrose, lactose and maltose.

Sucrose: prevalent in sugar cane and sugar beets, iscomposed of glucose and fructose through an (1,2)-glycosidic bond.

Lactose: is found exclusively in the milk of mammals andconsists of galactose and glucose in a (1,4)glycosidic bond.

Maltose: the major degradation product of starch, iscomposed of 2 glucose monomers in an (1,4)glycosidic bond.

Most of the carbohydrates found in nature occur inthe form of high molecular weight polymers called polysaccharides. The monomeric building blocks usedto generate polysaccharides can be varied; in all cases, however, thepredominant monosaccharide found in polysaccharides is D-glucose. Whenpolysaccharides are composed of a single monosaccharide building block, theyare termed homopolysaccharides.Polysaccharides composed of more than one type of monosaccharide are termed heteropolysaccharides.

Glycogen is the major form of stored carbohydrate inanimals. This crucial molecule is a homopolymer of glucose in (1,4) linkage; it is also highly branched, with (1,6) branch linkages occurring every 8-10 residues.Glycogen is a very compact structure that results from the coiling of thepolymer chains. This compactness allows large amounts of carbon energy to bestored in a small volume, with little effect on cellular osmolarity.

Glycogen Structure. Section of a glycogen polymer depicting glucose monomers as colored balls. The blue balls represent glucose linked by 1,4 glycosidic bonds. The red balls represent glucose at branch points where there are both 1,4 and 1,6 glycosidic bonds. The orange balls represent the reducing ends of the polymeric chains of 1,4-linked glucoses. The area in the box is expanded to show the actual structure of the glucose monomers in both -1,4- and -1,6 glycosidic linkages.

Starch is the major form of stored carbohydrate inplant cells. Its structure is identical to glycogen, except for a much lowerdegree of branching (about every 2030 residues). Unbranched starch is called amylose; branched starch is called amylopectin.

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Biochemistry of Carbohydrates

Department of Biochemistry and Molecular Biology | | UMass …

This year Biology, Biochemistry, and Core Facilities staff, students, and faculty collaborated on the Drug Discovery: Medicinal Properties of Plants course. This 2-week course shared the richness of the Plant Cell Culture Library as both a research and an educational resource with high school students in the UMass Summer Precollege program. This year our enrollment increased from 5 to 11, including several local students, 1 international student, and others from as far away as Texas and California. Students attended faculty lectures, propagated plants at the Morrill Greenhouse, visited research labs, pressed local plant specimens in the herbarium, designed primers, performed DNA extractions, PCR, agarose gel electrophoresis, and a disc diffusion assay, toured the Nourse Farms strawberry propagation center in Whately, designed and printed 3D models of plant metabolites, and presented their findings at a poster session in the Life Science Laboratories Conference Center. We are very proud of what our students have accomplished in 2 weeks and hope to see them on campus again soon. Thank you to all who supported our students' success in this course!

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UC scientist finds new solution to fight superbug infections – WCPO Cincinnati

CINCINNATI It only took years of studying, getting his PhD and completing post-doc positions at two universities for Daniel Hassett to land a job that eventually led him to discover a drug that can fight superbug infections resistant to antibiotics.

No, it's not a cure for coronavirus, but it's pretty darn cool. At least, that's what Hassett, a professor in the UC Department of Molecular Genetics, Biochemistry and Microbiology, will tell you.

Its actually beyond a big deal -- Its huge, Hassett said while standing in the laboratory where he made this discovery. The real plus of it is that it not only kills all of bacteria, but it kills the ones that are the most antibiotic-resistant bacteria.

Paola Suro

The bacteria he has been fighting makes about 2.8 million people in the United States sick every year and kills more than 35,000 people, according to the Centers for Disease Control and Prevention.

In very, very severe infections where the bugs are resistant to everything, its virtually impossible for them to become resistant to my drug, he said. Its not only anti-microbial, it has powerful wound-healing capacity as well.

Paola Suro

The invention called AB569 is composed of ingredients pacified nitrite and ethylenediaminetetraacetic acid and kills one of the most serious bacterium (Pseudomonas aeruginosa) that is resistant to several drugs and virulence.

Even if it positively affects one patient with a certain anomaly, just one, its a good thing, Hassett said. But we think its going to be pretty ubiquitous as far as this treatment goes.

Paola Suro

At first, researchers found AB569 could potentially treat antibiotic-resistant organisms that cause pulmonary infections in people with cystic fibrosis and chronic obstructive pulmonary disease, among others. Since then, Hassett said he has found it could do more than that, including treat urinary tract disorders, heal wounds, and even treat diabetes.

AB569 kills these pathogenic bacteria by targeting their DNA, RNA and protein biosynthesis as well as energy and iron metabolism at concentrations that do not harm human cells, he explained to UC Health researchers. These were tested in laboratory mice and humanized cells. Our data implicate that AB569 is a safe and effective means that could be applied to eradicate these superbugs.

Pseudomonas aeruginosa was placed in the lungs of lab mice for five days. It's considered one of the six ESKAPE pathogens, which, according to Hassett, are among the most resistant and deadly to humans. It includes Enterococcus faecium, Staphylococcus aureus, Klebsiella pneumoniae, Acinetobacter baumannii, Pseudomonas aeruginosa, and Enterobacter spp. These pathogens can result in infections and illnesses like pneumonia and MRSA.

Paola Suro

His discovery was patented in March 2018, but now he is working on getting more funding and support to push this discovery further.

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UC scientist finds new solution to fight superbug infections - WCPO Cincinnati

Itaconic Acid (IA) Market 2020 Outlook and Forecasts 2026 by Top Manufacturers, Production, Consumption, Trade Statistics, and Growth Analysis – News…

The Itaconic Acid (IA) Market report enlightens its readers about its products, applications, and specifications. The research enlists key companies operating in the market and also highlights the roadmap adopted by the companies to consolidate their position in the market. By extensive usage of SWOT analysis and Porters five force analysis tools, the strengths, weaknesses, opportunities, and combination of key companies are comprehensively deduced and referenced in the report. Every single leading player in this global market is profiled with their related details such as product types, business overview, sales, manufacturing base, applications, and other specifications.

Major Market Players Covered In This Report: Kehai Biochemistry, Guoguang Biochemistry, Huaming Biochemistry, Alpha Chemika, Zhongshun Science & Technology

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Itaconic Acid (IA) Market has exhibited continuous growth in the recent past and is projected to grow even more throughout the forecast. The analysis presents an exhaustive assessment of the market and comprises Future trends, Current Growth Factors, attentive opinions, facts, historical information, in addition to statistically supported and trade validated market information.

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Itaconic Acid (IA) Market Outlook by Applications: Plasticizer, Lubricating Oil Additive

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Coronavirus Ireland: What exactly is Covid-19 and what will happen next? Biochemistry expert Prof Luke O’Neill explains – Independent.ie

How can something so tiny be wreaking such havoc? SARS-CoV2 is the name of the virus that causes the new disease Covid-19, named on February 11.

t is so small that 500 million of them would fit on the full stop at the end of this sentence. David and Goliath, except David isn't even as big as an ant when compared to Goliath. And yet look what's happening. Economic turmoil. Cities and towns in quarantine. People not travelling for holidays or weddings. Sporting events cancelled. People who feel sick and who have met someone with the virus keeping themselves in isolation for 14 days. And the fear that the worst is yet to come outside China where it all started. That something so tiny can pack such a punch is a testament to how powerful viruses can be.

Viruses were first observed in 1948 with an especially powerful microscope called the electron microscope. The first members of the viral rogues gallery to be seen were the viruses that cause polio and smallpox. Both are highly contagious (around three-fold more than SARS-CoV2) and wreaked havoc in humans for centuries, paralysing us, disfiguring us and killing us. Then vaccines were developed and that put an end to that, with smallpox being eradicated completely and polio almost beaten.

Apart from being able to see them, scientists also figured out what viruses were made of. They have a coat made of fat, so they don't dissolve in water, although alcohol can dissolve them, which is why alcohol hand rubs are good at killing them.The alcohol dissolves the fat. Inside the fatty bag lies their genetic material - the recipe that can be read to make more virus. They also have proteins sticking out of the bag and they use these proteins to latch on to the cells they want to infect. A bit like a key, the protein fits into a lock on the surface of the cell the virus wants to infect and opens the door.

In the case of SARS-CoV2, the proteins occur on the end of the spikes that make the crown that surrounds them. This is why it's called a corona virus. They stick the spike key into a lock called ACE2 on your lung cells and the virus then gets inside. This is why it infects your lungs: that's where the ACE2 lock is.

It needs to get inside the cell to use it as a factory to make more viruses.

The ultimate parasite

Viruses are the ultimate parasite. As far as we know they bring no benefits. A bit like unwelcome guests who come to stay, procreate in your guest room having eaten all your food and drunk your wine, and then leave without saying thanks.

The recipe that SARS-CoV2 has to make more of itself is called RNA. This is why SARS-CoV2 is a bit like flu - the influenza virus also has RNA as its recipe, as do viruses that cause the common cold and Aids. There are plenty of types of RNA viruses.

Once it's made copies of itself, it leaves and moves on to another cell. The trouble is, it sometimes kills the cell it infected - the guests leave a bomb as they depart - and that's when the trouble can begin. You start to hurt. Influenza will kill billions of cells in your lungs in a typical infection, which causes fluids to build up making it hard to breathe. That can really irritate your lungs. And then you cough it out. The virus makes you cough because it wants to spread. The drops of spit fly through the air and land on surfaces where someone else picks them up and then touches their nose or mouth and the virus enters a new body. The unwanted guests have moved next door.

This is why it's important to wear a mask if you're infected since that traps the virus. And why the number one recommendation of the World Health Organisation is to wash your hands. And why it's good to clean surfaces if you've someone in your house who's infected. Wearing a mask doesn't seem to protect people much as they fidget with it or take it off a lot. And the virus can probably get in through your eyes anyway.

Natural defence

But now some good news. Luckily evolution has helped you. Your immune system is on hand to recognise the intruder and bring out the big guns to kill it. It's like you've got on your iPhone and called for the gardai to get rid of your unwelcome guests (if possible, before they have done the deed in your guest room).

The immune system has evolved all kinds of ways to recognise and eliminate the intruder. It has special sensors for the virus's RNA which set off the alarm. It can also detect the spike protein. Your immune system can make antibodies and these latch on and stop the virus getting into cells. A bit like putting blu-tack over the key. The antibodies also help immune cells eat the virus.

Your immune system even has a way of killing the virally-infected cell. This is almost like the gardai deciding to blow up your house. It is worth it because it stops the virus (or your guests) moving into other houses in your neighbourhood. Remember, they've multiplied. So blowing up one house saves many.

If you're healthy, your immune system works a treat. The gardai are well fed, have had a good night's sleep and have the weapons to do their job. And, once the job is done, they are highly experienced. Should the unwanted virus turn up again, they can recognise and kill it on sight. This is how vaccines work. They are weakened forms of a virus, or parts of it, which train the immune system so that when the real culprit comes along, the immune system is ready to attack and you are protected.

So what can go wrong?

In the case of Covid-19 (and influenza), people who are sick with other ailments (for example cancer or heart disease) can't mount a proper defense and so the virus runs riot. Their immune systems aren't up to the job because of the other illnesses they have. Sadly, this can mean fatalities which at this stage are around 2pc and mainly involve people with other illnesses. As we age, our immune system does, too, so this puts older people at risk. We therefore need a vaccine and huge efforts are going into that with the real hope that one will be available in nine-12 months.

Doctors are also testing medicines to stop the virus from harming us. Drugs used to treat HIV are showing promise; HIV is somewhat similar because it has RNA too.

A drug used to treat malaria called chloroquine is also showing promise, as are high doses of steroids. What these drugs do is interesting. Although the immune system is failing in people who get really sick, it turns out that one part is over-active. Because the virus is running rampant, it hugely provokes this part (called innate immunity) which causes a process called inflammation to kick off - this makes your temperature go really high and causes your lungs and other organs to fail.

What people actually die of is the friendly fire caused by this over-active inflammatory response which is sometimes called a 'Cytokine Storm'. Steroids and chloroquine put that fire out and so protect you.

It's a bit like where there were two unwanted visitors in your house, there are now thousands and the gardai get their batons out and go to work on them. A melee ensues and sadly in the violence and chaos you die. Not a good result. Steroids and chloroquine are like cold water being sprayed over the gardai.

What next?

SARS-CoV2 is a new virus so we have to be vigilant. The death rate is unlikely to go up and if anything might go down as more people are found to have fought it. It also mutates at a rate slower then say HIV or influenza so it can't change itself too readily.

This means that once your immune system recognises it and eliminates it, it will recognise it again. A change might also mean it becomes more toxic, killing more, but again this is unlikely.

It may well enter the community and become just another virus that causes flu-like symptoms that we learn to live with. It might weaken as it adapts to us. Killing us is in general a bad idea for a virus - it's like those guests... why would they kill you when they want to sponge off you again? Many will develop resistance and refuse the unwanted guests entry. And when we have a vaccine, the vulnerable can be protected.

Right now though, follow the guidelines. Isolate yourself if you have symptoms and have come into contact with someone with the virus and call your GP. No need if you don't meet these criteria. Wash your hands a lot.

Soap and water is fine -work up a good lather as viruses hate soap because it dissolves them. If you're vulnerable, don't travel to places where the virus is. We all just need to keep calm, remain vigilant and wait it out. This too will pass.

Luke O'Neill is professor of biochemistry in the School of Biochemistry and Immunology at Trinity College Dublin

Originally posted here:
Coronavirus Ireland: What exactly is Covid-19 and what will happen next? Biochemistry expert Prof Luke O'Neill explains - Independent.ie

UVM Appoints New Dean of Agriculture and Life Sciences – UVM News

University of Vermont Provost and Senior Vice President Patricia Prelock today announced the appointment of Leslie V. Parise, Ph.D., as dean of the College of Agriculture and Life Sciences (CALS).

Parise has built a long and successful career at the University of North Carolina-Chapel Hill (UNC-CH), where she rose through the ranks from assistant to full professor. For the past decade, Parise has served as the chair of the Department of Biochemistry and Biophysics, which currently ranks fifth in the United States for National Institutes of Health-funded biochemistry departments.

Dr. Parise is a strong proponent of translating research to benefit society, said Prelock. She impressed the search committee with her understanding of the importance of UVMs land-grant mission, and the critical role CALSand UVM Extensionhave played in advancing this mission. She has a track record of working with faculty to promote inventions, patenting, and licensing agreements. And her entrepreneurial mindset resonates with the innovative spirit so central to our UVM community. I have no doubt that Dr. Parise will be an exceptional leader and member of our community.

President Garimella said of her appointment, We are delighted that Dr. Leslie Parise is joining the University of Vermont as dean of the College of Agriculture and Life Sciences. She brings an impressive skillset to the university: great prowess in basic and translational research, longtime success promoting entrepreneurship and technology transfer, a commitment to student success, and a proven track record as a leader. We very much look forward to welcoming her to the UVM community.

Parise said she is honored to join the UVM community. CALS and UVM Extension play an incredibly important role in demonstrating the power of UVMs land-grant mission, she said. I look forward to meeting and working closely with the world-class faculty, staff and students of UVM, along with residents of Vermont. Finding ways to further engage our constituents to strategically maximize the educational, research and service missions of CALS, and to increase its visibility across the state and beyond will be among my priorities. I look forward to further positioning CALS as a microcosm for positive global impact.

Widely recognized for cardiovascular and cancer research, Parises work has been continuously funded, including more than $14.5M from the NIH. She is also a strong advocate for faculty and student advancement. As department chair at UNC, she worked with faculty, students and postdoctoral fellows to reinvigorate programs through a range of approaches including enhanced internal communication and planning, and increased mentoring.

Parise helped faculty maintain and grow funding through partnerships across campus and with neighboring institutions to facilitate greater investment from foundations and government agencies such the Keck Foundation, American Heart Association, National Institutes of Health and the National Science Foundation. She also facilitated partnerships with neighboring institutions to stimulate investment in a highly transformative technology for solving molecular structures called cryo-electron microscopy.

In 2017, Parise was elected Chair of the Faculty at UNC-CH, a role she held until May 2019. In this capacity, she represented all 3,800 faculty of the UNC-CH campus, interacting closely with the chancellor, provost, deans and faculty from within the university, as well as UNCs Board of Trustees, system president, and a faculty assembly from across the states 17-campus system. She has worked closely on issues ranging from curriculum changes, to budget models, to advancing diversity.

Parise will join UVM on May 15.

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UVM Appoints New Dean of Agriculture and Life Sciences - UVM News