Zombie Amoebas: Your Brain is at Risk

What would you say if I told you that there are brain-eating amoebas lurking in warm bodies of water, capable of entering your body through your nose? Would you ask what an amoeba is? Would you ask why it wants to eat your brain? Would you decide to boycott outdoor water parks for the rest of your life?

Naegleria fowleri
Credit: Wikimedia Commons. This image is part of the public domain.

Not to worry, these amoebas do not intentionally set out to eat your brain. However, they are capable of causing a fatal infection upon entering a human body, so it is important to be aware of their existence as well as practices that can help prevent disease.

First, some background information. An amoeba is a single-celled organism that is capable of moving around by projecting pseudopodia or “false feet”. It can use its cell membrane to engulf food particles through a process called phagocytosis.

More specifically, the “zombie amoeba” itself is a species called Naegleria fowleri. It was first discovered in Australia in 1965.

Naegleria fowleri thrives in warm waters – it can survive in temperatures of 45 degrees Celsius! Areas in which the organism is commonly found include warm lakes or ponds, mud puddles, slowly moving rivers, pools or spas that are not chemically treated, hot springs, aquariums and soil. Some good news, however: Naegleria fowleri cannot survive in salt water or in swimming pools that are correctly chemically treated, so you don’t have to stop frequenting your local swimming pools or the beach.

Click on the video below for more information about Naegleria fowleri

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Credit: Centers for Disease Control and Prevention, Wikimedia Commons. This work is in the public domain.

As stated previously, the term “zombie amoeba” is actually slightly misleading, as the organism does not actively seek out human brains as a food source. According to the Centers for Disease Control and PreventionNaegleria fowleri normally feeds on bacteria. The organism may enter the nose during activities such as swimming and diving. Once it has entered, the amoeba travels to the brain where it feeds on brain tissue, causing swelling and ultimately, death.

These infections occur most frequently in the southern United States during warmer months. The name of the infection itself is primary amebic meningoencephalitis (PAM), the symptoms of which are: headache, fever, nausea, vomiting, neck stiffness, confusion, balance problems and seizures or hallucinations. Rapid progression of the disease can lead to death within an average of 5 days.

Changes observed in body tissue as a result of PAM. Source: Wikimedia Commons. This Image is part of the public domain.

However, according to the CDC:

“Naegleria fowleri infections are rare. In the 10 years from 2008 to 2017, 34 infections were reported in the U.S. Of those cases, 30 people were infected by recreational water, 3 people were infected after performing nasal irrigation using contaminated tap water, and 1 person was infected by contaminated tap water used on a backyard slip-n-slide.”

To prevent infection, the CDC recommends focusing on keeping water from entering your nose by abstaining from diving headfirst into water or submerging your head. As well, it is a good idea to avoid stagnant bodies of water. There is no effective treatment for PAM at the moment, so more research needs to be done so that this disease can be stopped from claiming more lives.

Maya Liepert

 

 

 

Echolocation: How Two Seemingly Polar-Opposite Creatures Developed the Same Highly Specialized Skill

Have you ever been walking through your house in the middle of the night with all the lights off, searching for a glass of water, but you feel an intense pain running through your body as you stub your toe on the counter? This would never happen if humans had echolocation: the ability to map out the area ahead of you by using reflections from high-pitched sonar signals.

Animal Echolocation
Credit: WikiMedia

Echolocation is an ability that is primarily used by dolphins and bats. This raises the question, why is it that dolphins: hairless mammals which live in the ocean, happen to have the same specialized ability as bats: which are furry, nocturnal, and flying critters?

Dolphins utilise a unique organ called the melon to send out high frequency clicks. They have a large depression in their skull to make space for this organ, allowing them to produce bisonar for orientation. Beyond this, echolocation gives dolphins an idea on the object’s shape and size, although it is not quite understood by scientists exactly how this happens.

Bisonar by cetaceans
Credit: Wikimedia

Bats dominantly use a method of echolocation called laryngeal echolocation, which is characterized by the production of very short wavelength sounds from their larynx. The connection between their stylohyal bone and tympanic bone enables the bat to neurally register and separate outgoing and incoming ultrasonic waves. They have evolved to differentiate between the pulses they produce and the echoes that they receive back.

Ventral view of the Florida Freetail bat, highlighting the tympanic and stylohal bones. Credit: Pacific Lutheran University Natural History 

This skill could potentially be relevant for humans today, as researchers are using this skill to test human echolocation in blind people. It has been revealed that some blind people were able to independently develop a type of echolocation, by utilising sound, they are able to map out the space they are in and develop an image of it for themselves. Some researchers are studying this ability, attempting to make it accessible for all who might need it.

So how is it that dolphins and bats have developed these extremely similar skills? Clearly, there is the fact that because dolphins hunt in murky ocean waters, and bats hunt late at night in the dark. Thus they both had to have evolved some method to cope with the darkness, but why was it that they developed the same method of echolocation independently? A team of scientists were trying to answer this question, and a paper in Science Advances announced that there exist genetic characteristics that could have helped dolphins and bats both develop this skill.

This international group of scientists searched through the genomes of each animal, searching side by side for any similarities in amino acid sequences. They found that bats and dolphins share amino acids linked to proteins involved in the development of a very specific set of fast-twitch muscles. These were the muscles that drive the “terminal buzz”, or the rapid high frequency calls that bats and dolphins both make when hunting.

Figure showing sudden increase in high frequency calls in a bat
Credit: The Gall Lab

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Sound clip of terminal buzz – the terminal buzz is the last pulses of an echolocation call sequence: and will speed up at the end because the bat is getting closer to the object it is interested in.
Credit: The Gall Lab

This similarity in amino acid sequence may be a part of what helped these two very different animals develop the same skill, but there is still plenty to uncover about the specifics of how dolphins and bats developed echolocation independently. However, we are much closer to uncovering this mystery than in the past.

Jin Kyu Lee

Fiberglass-spinning robots could be construction workers of the future

Similar to how a silkworm spins a cocoon from a single thread, there is a new man-made robot that also creates things from a single thread. The only difference is that while a silkworm builds a cocoon for a home, the robot builds custom-shaped fiberglass structures for further construction.

Robots that can spin fiberglass thread. Their silicon balloons are shown on the left and the various types of fiberglass structures formed are shown on the right. Source: Science News

Once programmed, these robots are capable of building woven fiberglass tubes that can create large structures such as buildings and bridges, without the continued help of humans. Because they can be independent after being programmed, the robots become especially useful when it comes to infrastructural development in areas where humans cannot go.

Down below is a video of how these robots build fiberglass structures.

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When it comes to size, these robots are only a little bigger than a 1-liter bottle. This is including the silicone balloon with propeller arms located on the top of the robot. These “arms” are primarily used to build fiberglass structures by producing a resin-coated thread, which is then hardened through ultraviolet light. As a result, the threads are glued into one larger piece that is usually at a length of 9-centimeters. Once formed, the silicone balloon deflates and tilts to bend the segment into different shapes and sizes.

The components of the Fibreglass Spinning Robots. Source: Archpaper

Markus Kayser, a designer and roboticist at MIT, and his colleagues tested the fiberglass structure made by the automated robots. They found that the structures could withstand cold weather for up to seven months without any damage. In addition, they have found that the robots could join other construction robots to build more complex structures.

Robots building tube-shaped fiberglass structures in extreme weathers. Source: Science News

One limitation is that because these robots receive orders from a computer, they can only create pre-registered and pre-designed infrastructures. However, as these machines advance in technology, there is a high possibility that they will be capable of doing much more. There is hope that they may even be part structural development in areas such as underwater or even on other planets.

The disease which turns you into a statue, FOP

We all know the story of Medusa, the serpent lady who can turn other life into stone statues of themselves, but what if I told you there is a disease that works similarly and results in the infected individual becoming absolutely immobile. Fibrodysplasia ossificans progressiva (FOP) is an extremely rare disease which affects only two individuals per one million people. FOP is caused by a mutation in the ACVR1 gene, which results in the wrong bonding shape of the protein responsible for rebuilding muscles so that bone and cartilage material are instead accumulates. When a FOP patient suffers damage to muscle tissue, bone matter builds on the injured area and hardens to form solid material. Signs of FOP can be seen at a early age, as patients develop distinct big toe joints that are aimed inwards.

 

The foot of a FOP patient; the toes are aimed inwards and have a distinct shape.http://fopaustralia.org/wp-content/uploads/2016/01/Child-toes.jpg

Jailed by Yourself

Imagine getting stuck within the confinements of your own body. Everyday, a part of your body would stop working. You will soon not be able to even lift your hands up to scratch your head. The only escape is death. This is exactly what a FOP patient is feeling throughout their life. Unfortunately, there are no cures for this type of disease. Bone removal is an option but it just delays the inevitable. Patients are advised to not move strenuously to minimize the muscle damage.

A video of a FOP patient is linked below:
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Victims of FOP 

The most famous of all FOP cases would be the case of Harry Eastlack. His condition came to light after he broke his leg which later hardened as the muscles in his legs became bones. Many more injuries later, Harry’s skeleton have morphed together, his vertebrae being one piece and most of his joints have fused. After he died from pneumonia, his body was donated to science and is now displayed at Mutter Museum.

The skeleton of Harry Eastlack; he froze in place, the same way he lived for the last few years of his life.https://www.raredr.com/news/physician-recommendations-fop

Hyperlink to sources: https://www.ifopa.org/what_is_fop, https://ghr.nlm.nih.gov/condition/fibrodysplasia-ossificans-progressivahttps://www.webmd.com/children/what-is-fop

The Calm Before the Flood: Glacial Lake Outbursts in Bhutan

When you think of global climate change, what is the first thought that comes to mind? Species extinction? Rising ocean levels? Extreme weather events?

It turns out that all of these are possible, unfortunately! However, one that is often overlooked is the formation of supra-glacial lakes. As temperatures rise, the rate of ice melt has accelerated and has increased the amount of water in glacial lakes. Once triggered by an earthquake or ice fall, the lake will overflow. To make matters worse, the melting of ice-core dams can also destabilize the lakes, forming Glacial Lake Outburst Floods (GLOFs). This means that all communities downstream of glacial lakes are at risk of flooding! An example of this is Bhutan – a landlocked country in South Asia.

A map showing the topography of Bhutan and surrounding countries.
Image Credit: Wikimedia Commons

As you can see, Bhutan consists of rugged land with steep mountains. Most of Bhutan’s population resides in large river valleys, making their lifestyles vulnerable to flooding. Bhutan’s society is not prepared to deal with flooding, since they rely upon their agricultural sector and hydropower as a source of employment and revenue.

A graph showing the recent trend in GLOF in Nepal, Bhutan and Tibet.
Image Credit: Flickr, User GRID Arendal; published under the Creative Commons License.

To lower the risk of flooding, Bhutan’s first project is in the most dangerous glacial lake: Thorthormi Lake. The goal is to create a channel to drain water out of the lake, which is accomplished by releasing pressure on the dam and using tools to dig ice and remove boulders. So far, the lake has been artificially lowered slightly, increasing the safety for downstream communities. The importance of this project and the necessity for further glacial satellite observation is addressed in the video below.

A video about Bhutan’s melting ice, in the perspective of a world exploration challenge.
Video Credit: Vimeo, User Skyship Films, published under the Creative Commons License.

Bhutan is only one example of a community that is directly threatened by climate change. Therefore, we must invest more thought and research into climate change induced disasters, since preparation is key and can offset future damage.

 

Lexynn Kwan

Link

Integrating Peptides into RNA-World

Integrating Peptides into RNA-World

The RNA-World

Over 4 billion years ago, the molecular precursors to life showed up in the inhospitable soup of chemicals that we can barely recognize as Earth. The identity of these first molecular precursors is a schismatic “the chicken or the egg” debate, splitting people between groups that support molecules that carry information and ones with enzymatic activity.

If only a family of molecules could both have enzymatic activity and contain genetic information. Thus we enter the “RNA-world”, RNAs are molecules with its unique properties of having enzymatic activities and contain genetic information, it is the perfect molecule to self-replicate and mutate to pave the way for peptide and DNA to take over each role more effectively. This was the widely accepted theory since the 1960’s and remain relatively unchallenged until recently.

File:Geological time spiral.png

The timeline of the biodiversity of Earth, it all started with a few molecules. Image Credit: United States Geological Survey

The Problems of RNA-World

An article in Biosystems and another in Molecular Biology and Evolution, showed why a peptide-RNA complex world view is better than RNA-world hypothesis at explaining what the primordial molecular precursors would look like.

The researchers, Charles Carter from the University of North Carolina and Peter Wills from University of Auckland, from the articles approached the subject from two angles. First, from the perspective of enzymatic activity, although RNA show enzymatic activity but RNA does not react well to change like proteins. As a result, in the environment 4 billion years ago when the sea was cooling rapidly, the only way enzymatic activity could have survived was through proteins.

The other problem was genetic information, because at the beginning there were no genes or genetic codes. The changes and mutations in RNA would only be reflected in its abilities as an enzyme. An RNA only world cannot explain how and why the changes in RNA would lead to the creation of a genetic code with the purpose to create proteins. Thus, leaving a gap between the RNA world to the protein and DNA world.

The Peptide-RNA World

They proposed that a peptide-RNA complex, with the peptides that contain enzyme activity and RNA for genetic information, would fill the gap that the RNA-world cannot explain. This relationship would directly explain how mutations in RNA would affect enzymatic activity in protein, and why it needs to create better proteins to protect itself from a wider variety of situations. Furthermore, the addition of proteins explain how the first molecular precursors could survive in the ever-changing climate of the relatively new Earth.

https://upload.wikimedia.org/wikipedia/commons/e/e2/Protein_mosaic.jpg

A protein mosaic, providing an insight on the complexity of proteins. Image Credit: Astrojan

When the proteins and RNA were joined together at the start of life, the mechanisms for construction through transcription, translation, and replication must have co-evolved. With this concept in mind, the researchers found commonalities between compounds similar to evolution from a common ancestor. Thus, with these concepts in mind, when looking at molecules we can find an evolutionary chain to see how molecules developed to be what it is today and also why they developed this way.

Finally, to answer the “chicken and the egg” debate, it is likely to be both like an Oyako-Don (mother-child bowl), a Japanese dish that harmonize chicken and eggs. Life as we know it was likely developed through a combined effort of RNA and proteins.

Are we putting ourselves at risk by driving without that extra hour of sleep?

It’s no secret! We have all had those days when “I’m so tired” is the only piece of conversation we can contribute. But has being tired ever stopped you from driving your car? Recently, there has been an increase in research showing fatigue to be a major contributing factor in motor vehicle accidents. According to The National Highway Traffic Safety Administration of the USA, there was 4,121 fatal crashes between 2011 and 2015 involving drowsy driving. This has led researchers to explore the idea of establishing methods for discouraging people from driving while in a lethargic state and for catching them in the act.

Driving Tired

Drowsy driving can be risky
Image Source: flickr
Photographer: Anna~Bee

 

Does being drowsy really affect me?

We can all relate to being tired every now and again, whether it is a busy week at work, a heavy class schedule, or even as a result of a sleeping disorder. What we do not always realize is the very real effects that even the smallest lack of sleep can have on our bodies. In fact, research done by the AAA Foundation for Traffic Safety, shows that even just one or two hours of sleep less than the recommended within 24 hours, can double the risk of collision. Some of the effects of drowsiness are, but are not limited to, the following:

  • Trouble focusing
  • Heightened risk-taking
  • Impaired attention
  • Changes in mood

Accident

Fatal accidents caused by drowsy driving
Image Source: flickr
Photographer: Thomasjuh-b

 

Wait! How do you know how drowsy I am?

Now, what if I told you that police officers could test your sleep level, as they would alcohol levels, if they saw fit? Would you think twice about getting behind the wheel? This is the end goal for researchers from the Sleep Research Centre at the University of Surrey, who were working towards developing a biomarker capable of assessing an individual’s sleep level. A study was conducted where 36 participants were subjected to a 40-hour period of sleep deprivation. During this time, researchers drew blood from participants in order to observe any changes their lack of sleep would have on the expression levels of their genes. This study resulted in a major breakthrough in the form of an algorithm, which can be used to test blood samples for sleep deprivation with 92 percent accuracy. This breakthrough not only paves the way towards a future with a test capable of checking for sleep-deficient drivers, but also emphasizes the extent of the physiological impact a lack of sleep can have on our bodies, made evident by the fact that these biomarkers are present in the subject’s blood only after a 24-hour period.

Observing driving behaviour of drowsy drivers
Posted By: Mobilegeeks.de

 

Evidently, lack of sleep can have major influences on our bodies and is a serious contributing factor to fatal car accidents. While researchers are working towards methods to help society enforce regulations on sleep level while driving, we can all do our part by being more aware of our state of well-being before taking the wheel.

 

Shadi Elmi

Gut Bacterium Puts an End on Desperate Search for Type-O!

Long quest of the universal blood type

The idea of an ultimate universal blood type have dragged many intrigued life scientists into decades-long search for a routine productive type-O conversion. Now UBC’s Prof. Withers says his Lab made a leap towards the clinical use of universal blood group.

(Getty images; BBC )

So what is a blood type?

Since the discovery of quadruple blood types A,B, AB and O, medical scientists and a bit later immunologists have shared a long trail of hopeless struggle with the blood transfusion challenges. Recipient’s intense and potentially life-threatening immune responses are triggered by administering the incompatible blood types. The basic distinction among these blood types is the so called chemical molecules, so called markers, on the surface of the red blood cells; type-O red blood cells, however, completely lack these markers and thus could be safely transfused regardless of recipients’ blood types. In the case of type-O, the recipient’s immune system will not respond because it detects no markers on donor’s red blood cells.

(Kristine Ho;ubyssey website)

Pioneers of universal blood type

Back in 80’s, scientists took the initiative to remove those signatures from A, B and AB red blood cells, using a few enzymes, and turn these types into type-O to make it available to everyone in need particularly in emergency scenarios where there is a critically limited time to characterize patient’s blood type. The biggest obstacle, though, was impracticality and inefficacy of use of then-candidate enzyme. Besides, there was no technique for mass production of the key enzyme at the time.

And … the leap of faith!

UBC Withers’s Lab recently gained promising results by manipulating a number of common signature-removing enzymes that made the invented enzymes more robust and efficient than original ones. The new enzymes are found in a gut bacterium and was easily modified in this bug. The newly found enzymes have shown a significant competency in removing the red blood cell signatures. The last barrier to overcome is to enable this enzyme to cut out remaining forms of signatures in A and B red blood cells. Everything worked out in the laboratory, yet Withers group now looks into potential side effects and safety facets of their achievement.

by: Jamaledin Adel