Welcome back to The Vitals Podcast; I’m your host, Chauncey, back yet again to digest and bring you the latest in medical news today. It is Monday, May 27, 2024, and I have even more innovations to dig through with you. As always, don’t forget to follow the podcast and share it with your friends to keep everyone you know updated on the latest medical breakthroughs.
Created by Nadia Jaber with Biorender.com
Our first study comes from Dr. Ajay Goel and his colleagues at City of Hope Cancer Center in Duarte, California, who have perfected a blood test to detect pancreatic cancer early.
Pancreatic cancer, specifically pancreatic ductal adenocarcinoma (PDAC), is a rather tricky cancer; in early stages, it doesn’t present with any conspicuous symptoms, and established tests to check for it aren’t incredibly reliable. Catching it early, however, is a key factor in the cancer’s prognosis; chances of living for at least five years after diagnosis drop from 44% in early stage disease to only 3% in late stage. There’s a need for an accurate and simple test to detect early stage cancer, and Dr. Goel may have provided.
The blood test, called a liquid biopsy, developed by Dr. Goel detects tumor-derived exosomal micro-RNAs; that’s a mouthful, so let’s break it down. Micro-RNAs are a special type of RNA that serves as a translation regulator. Translation is the process of turning mRNA into protein. Micro-RNA splices or destabilizes mRNA so that it only makes as much protein as needed. Micro-RNAs are also sent between cells to regulate each other’s translation, acting as tumor suppressors, OR as messages between cells. To do this, they’re excreted out of the cell through a small sac called an exosome, making the micro-RNAs inside ‘exosomal micro-RNAs’.
The micro-RNAs that are released from cancerous cells (or ‘tumor-derived exosomal micro-RNAs’) are unique in that it, firstly, disrupts the immune system and its ability to attack the cancer, and secondly, acts as oncogenes, meaning it potentially promotes cancerous growth. More importantly, however, these exosomes essentially send away a small piece of the cancerous cell it came from, which can be collected and used to diagnose patients. This is the idea behind the liquid biopsy.
Testing this in a cohort of 95 individuals from Japan and the US, some with PDAC and some healthy, they reported a 98% detection rate. They continued this study using a larger sample size from three nations: the United States (139 with PDAC; 193 healthy donors); South Korea (184 with PDAC; 86 healthy donors); and China (50 with PDAC; 80 healthy donors). The detection rate here was 93% in the U.S. cohort; 91% in the South Korean cohort; and
88% in the Chinese cohort. In contrast, a test looking for an antigen called CA19-9 is only 86% accurate. Using data from the U.S. cohort, combining both tests together reported to be 97% accurate.
This test is a new tool in the battle against not only PDAC, but other cancers as well. Detecting the disease early is imperative to outcome and treatment, so this test will prove invaluable to the well-being of cancer patients.
Colorized transmission electron micrograph of H5N1 virus particles (gold), grown in epithelial cells. Microscopy by CDC; repositioned and recolored by NIAID.
Our second study comes from researcher Lizheng Guan and his team of colleagues at the University of Wisconsin-Madison and the Texas A&M Veterinary Medical Diagnostic Laboratory who are assessing the risk of infection from a pathogenic strain of avian flu through contaminated cow milk.
In recent news, at least two cases of Highly Pathogenic Avian Influenza H5N1 virus (or HPAI H5N1) have been recorded; one in Michigan and one in Texas. Both cases are of farm workers exposed to infected dairy cattle, or cows. Strangely enough, the patients have complained of symptoms in line with an eye infection, namely conjunctivitis, or pink eye; an eye swab of the Michigan case revealed it to be H5 Bird Flu, the name given by the CDC.
Additionally, a nasal swab was taken from the Michigan case, and came up negative. The CDC has added conjunctivitis as an official part of the virus’s case description next to normal flu symptoms. It also lists the public health risk as low because, firstly, the virus is not very transmissible from human to human, and secondly, the initial leap from cow to human is believed to have come from contaminated unpasteurized milk spilling on the patients’ hand, which they may have touched their eyes with. Milk from infected cows must be disposed of, and even so, milk is pasteurized at 72°C (~145°F) for at least 15 seconds, or 63°C (~161°F) for at least 30 minutes before being packaged.
The study conducted by Guan and his team saw them feed droplets of raw milk from infected cows to five mice. On Day 1, they showed signs of infection. They survived to Day 4 and were euthanized to determine their organ virus levels. The researchers discovered high levels of virus in the mice’s nasal passages, trachea and lungs and moderate-to-low virus levels in other organs, as expected.
They then tested to see which temperatures and time intervals were most effective at inactivating the virus in raw milk. Four milk samples with confirmed high virus levels were tested at 63°C for 5, 10, 20 and 30 minutes, or at 72°C for 5, 10, 15, 20 and 30 seconds. Each of the time intervals at 63℃ successfully killed the virus. At 72℃, virus levels were diminished but not completely inactivated after 15 and 20 seconds. In a separate experiment, the researchers concluded that the H5 virus can also remain infectious for several weeks in raw milk kept at 4°C (~39°F).
Overall, the researchers summarized that contaminated milk poses a risk when consumed untreated, and points out that the lab experiments of heating milk do not replicate the conditions at industrialized pasteurization facilities. As for the H5 Bird Flu in humans, the CDC is committed to keeping an eye on its activity until further notice.
Now, it is time for THE VITALS, where I go in-depth on what you need to know about topics of your choice. If you’d like your question to be answered, drop it down in the Q&A, and you may see it in a future episode!
This episode’s vital question comes from Kings, who asks, “How have robots integrated into the medical field?”
Great question, Kings. When we think of robots in medicine, we think of the more recent automated systems on the practitioner side; that is, robots for dispensing medication, transporting patients, patient screening, sterilization, and on and on and on. There are also robotic systems for pacemakers, ventilators, prosthetics, and imaging. In fact, the first robot used in medicine, PUMA 560, was for a brain biopsy way back in 1985 using robotic precision to eliminate human error. In 1988, PROBOT helped surgeons during prostate surgery; systems like Neuro-Mate, Minerva, and the Robot-Assisted Microsurgery System were made in the 1990s. In 1992, ROBODOC assisted practitioners during a leg operation. Many robotic systems that are used in medicine today were invented and approved in the 2000s.
Laparoscopic surgery is the opposite of open surgery; instead of cutting open a patient, surgeons poke holes into the patient’s abdomen, insert a small camera called a laparoscope, pump the abdomen with air, and insert small surgical tools to carry out the procedure with minimal risk. In 2000, the first Da Vinci Surgical System was approved by the FDA for general laparoscopic surgery. The newest system, the Da Vinci Xi was developed in 2018 and still is in wide use today. Intuitive Surgical, the developers of the Da Vinci Xi, are planning to release the Da Vinci 5 in 2025, using the newest and latest technology.
The Da Vinci Xi works like an extension of the surgeon’s hands. The robot has four arms, three of which can hold many different surgical tools, and a fourth that holds the system’s 3D cameras. The surgeon operates with the Da Vinci by using instruments that they guide via a console. The Da Vinci system translates the surgeon’s hand movements at the console in real time, bending and rotating the instruments while performing the procedure. The tiny wristed instruments move like a human hand, but with a greater range of motion, which allows the Da Vinci Xi to be used for a wide range of surgeries.
Thanks, Kings, for the question!
That’s all for this week’s episode, so thank you for tuning in, and a special thank you to my friend Nilesh for sharing your experience with us! Follow the podcast and share this episode with your friends! If you’d like your questions answered, remember to drop a response in the Q&A section of this video. Until next time, keep your vitals strong and your spirits high. This is your host Chauncey signing off. Take care and stay healthy, I’ll see you next week!
Anxiety weighs down the heart, but a kind word cheers it up.
Welcome back to The Vitals Podcast; I’m your host, Chauncey, back yet again to digest and bring you the latest in medical news today. It is Monday, May 20, 2024, and I have even more innovations to dig through with you. As always, don’t forget to follow the podcast and share it with your friends to keep everyone you know updated on the latest medical breakthroughs.
Dr. Elias Sayour (left) and his colleagues Chong Zhao (middle) and Arnav Barpujari (right) discussing the mRNA vaccine.
Our first story comes from Elias Sayour and his team at the University of Florida, who are testing a vaccine that teaches the immune system to attack the deadliest and most aggressive form of brain cancer.
Glioblastoma is extremely aggressive and particularly deadly. How deadly? Here are some facts: of the recorded cancer cases that affect the central nervous system (that is your brain and spinal cord), 45.2% are glioblastomas. Only 5.6% of adults affected have survived for at least five years after diagnosis; the median survival time for adults is 15 months. Treatment for this type of cancer involves surgical removal, followed by radiotherapy and chemotherapy, but it often comes back. But Sayour and his team may have a solution.
Now, there is a lot to unpack on how this works, so please bear with me here, but it all revolves around something called mRNA. Most of us know what DNA is; the information in our cells that tell them what to do by building proteins. Well, the DNA itself doesn’t go around and interact with machinery in our cells, just as builders don’t carry around the original blueprints; they take a copy to the construction site. Similarly, your cells house and protect your DNA, copy it, and send that copy out to build proteins. This copy is called mRNA. Here’s a fun bit of trivia, the “m” in mRNA stands for “messenger”.
Well, just like human cells, viruses have genetic code in the form of RNA. When they infect a cell, the viral RNA mimics our cell’s mRNA, forcing the cell’s machinery to build more viral proteins and viral RNA, which are then assembled and released to infect more cells.
Let’s take a breath here; to recap, our cells copy DNA to build proteins, and this copy is called mRNA. Viruses, like measles for example, carry viral RNA, which code to build viral proteins instead. Now, simplifying things a bit, your immune system “discovers” these viral proteins on the viruses and rallies an immune response, but takes a bit of time and allows the infection to make you sick before dispelling the pathogen. Once you do get better, however, it’s really unlikely you’ll get sick with the same virus again because your immune system will, in a way, “remember” this virus.
Vaccines take advantage of this by introducing a small, specific bit of that viral RNA into your bloodstream; let’s say measles again. This viral RNA will code for the proteins normally on the outside of a measles virus, proteins that your immune system can “discover.” When it enters and hijacks a healthy cell, it does NOT kill the cell, and the cell only builds and releases these bits of “discoverable” viral proteins, which your immune system promptly “discovers.”
The difference here is that the viral proteins aren’t a full-fledged measles virus, which means they aren’t enough to infect you and make you sick, but are enough for your immune system to “remember” the measles virus. That’s what immunity is. That means when the real thing comes along, your immune system can react much, much quicker.
What does ANY of this have to do with cancer vaccines? Well, Sayour’s method of treatment is surgically removing some of the glioblastoma (remember, that’s a brain tumor) from their patient (let’s call him Bob), extracting mRNA from the tumor sample, packaging it like a virus, and injecting it into Bob’s bloodstream. Essentially, they use lipid nanoparticles (small fat particles) to wrap around the RNA, which then codes for “discoverable” proteins made by Bob’s cancer cells. Bob’s immune system discovers the proteins and rallies an immune response. The difference between THIS and a viral vaccine is that the threat — Bob’s cancer — is still in Bob’s body.
So in reacting to a fake virus injected into Bob’s bloodstream, Bob’s immune system will also attack Bob’s glioblastoma as well, and hopefully, kill it. This process is replicated with Jane, with Jane’s unique glioblastoma, leading to Jane’s unique vaccine, spurring on Jane’s unique immune response.
Sayour’s team already observed the efficacy of this through animal clinical trials using 10 pet dogs that had glioblastomas (of course, at their owner’s consent). Normally, without treatment, their median survival would be 30-60 days. With this form of mRNA vaccination, the median survival was 4.5 months.
Using a group of four adult patients with glioblastomas, they did the same thing, and while it is too early to tell the results of this vaccination in humans, Sayour notes that, “In less than 48 hours, we could see these tumors shifting from what we refer to as ‘cold’—very few immune cells, very silenced immune response—to ‘hot,’ very active immune response.” If this is successful, the next step is moving to human clinical trials with more adults and children to confirm a correct dosage, and then to continue trials with pediatric patients.
This new, promising vaccination, if it’s safely tested in trials, could save a multitude of lives. Better yet, the potential this concept has to be replicated with other cancers (like lung cancer, the deadliest cancer in the US) brings us hope for what’s in store for humanity in the future.
Our second story comes from Dr. Bryan Roth, the director of the NIMH Psychoactive Drug Screening Program at the University of North Carolina School of Medicine, who is working with his team of colleagues at UCSF, Stanford, and Harvard to prove the effectiveness of an AI that can give you potential drugs to treat neuropsychiatric diseases.
AlphaFold2 is an AI system that can model protein structures, and in your brain, there are a LOT of proteins. For example, your neurons, the cells that send messages back and forth, have receptors to receive neurotransmitters; receptors are made of proteins. One type of receptor is called a ligand binding site; neurotransmitters bind to these sites, which (and I’m simplifying here) will have some type of effect. These sites are often the target for psychiatric drugs, which will also have some therapeutic effect.
Recent studies have doubted the accuracy of AlphaFold2 when modeling ligand binding sites. So, Dr. Roth and his team decided to put this to the test.
AlphaFold2 works by referencing a huge database of proteins and their structures, which it can then use in simulations as targets for molecular compounds (like new potential drugs). Scientists can observe the simulated effects, learn how the binding site works, and develop even more drug candidates.
The AI can do this in two ways: retrospectively, which means it tells you of a binding with a protein it already has plenty of information on, or prospectively, which means it receives a completely new protein to assess and test against drug compounds. This study examined AlphaFold2’s prospective abilities.
The researchers first fed the AI the structures of sigma-2 and 5-HT2A, two receptors important in cell communication. Complications involving these receptors have been implicated in neuropsychiatric conditions such as Alzheimer’s disease and schizophrenia.
Researchers determined that the proportion of compounds that actually altered protein activity for each of the models were around 50% for the sigma-2 receptor and 20% for the 5-HT2A receptor. For reference, a result greater than 5% is exceptional. What’s more, out of the hundreds of millions of potential combinations using the sigma-2 receptor, 54% of the drug-protein interactions modeled by the AI were successfully activated, similar to the 51% success rate of the control model.
AI is becoming a part of plenty of fields, and medicine seems to be one of them. With this promising data, AlphaFold2 and other AI programs like it could be honed and perfected to help develop better and better treatments for us non-robots around the world.
The COVID-19 pandemic devastated the world. (By CDC on Unsplash)
Now, it is time for THE VITALS, where I go in-depth on what you need to know about topics of your choice. If you’d like your question to be answered, drop it down in the Q&A, and you may see it in a future episode.
This episode’s vital question comes from Pete, who asks, “How are we dealing with COVID in 2024?”
Great question, Pete. We all know about the COVID-19 pandemic that lasted from 2020 – 2023. This disease has taken the lives of approximately seven million people worldwide, 1.2 million of which were in the United States according to WHO. It shut down schools, childcare, and businesses, and cost the US economy an estimated $14 trillion in net economic output, according to USC.
Vaccines made by Pfizer, Moderna, and AstraZeneca all rolled out on Emergency Use Approval (EUA) in December of 2020, and Johnson & Johnson rolled out their vaccine in February of the next year, and in both clinical trials and the real world, proved to be effective against COVID-19. According to WHO, as of the last day in 2023, 70% of the United States population is fully vaccinated, and 82% of Americans have at least one dose of a COVID-19 vaccine. So why do we still have COVID-19 going around?
I’m sure you’ve heard what variants are. There’s the Alpha variant, and the Delta Variant, and the Omicron variant, and so on, but what is a variant, and how do they occur?
Remember when we were talking about viruses having genetic code? Well, when it makes more copies of itself, it sometimes makes mistakes. Actually, it makes a lot of mistakes. When they happen in the virus’s genetic code, that’s called a mutation. When a virus mutates enough (when the “discoverable” proteins are different enough), the weapons in your immune system do not recognize it anymore. Essentially, the immune system treats it like a whole new virus, starting the immunity process again. This is what variants are; viruses mutated from the original virus.
Many viruses mutate, but some are more prone to mutate than others. For example, Rhinoviruses (the viruses that cause the common cold) and Influenza viruses mutate often, which is why there are so many variants that can get you sick. Viruses that cause smallpox, chickenpox, and measles all mutate a lot less, which is why when you catch these infections, it’s unlikely you catch them again.
COVID-19, in comparison, mutates a lot, hence the variants and subvariants of seemingly the same virus, and the many vaccinations and boosters to combat them.
Fun fact before we close, though; no matter the variant, thoroughly washing your hands with soap and water, and coughing or sneezing into your elbow will always prevent the spread of infection!
That’s all for this week’s episode, so thank you for tuning in! Follow the podcast and share this episode with your friends! If you’d like your questions answered, remember to drop a response in the Q&A section of this video. Until next time, keep your vitals strong and your spirits high. This is your host Chauncey signing off. Take care and stay healthy, I’ll see you next week!
Before we start, a quick announcement; I have a podcast! If you’d like to listen to these stories and more, including The Vitals, where I tell you what you need to know about topics of your choice, tune into The Vitals Podcast on Spotify, or wherever you get your podcast! Sources to each story are below!
Counting atomic ratios in yeast and mouse cells to study cancer clues
Our first story comes from researchers Ashley Maloney and Sebastian Kopf and their joint research team made up of scientists at Colorado University and Princeton University, where tools often used in geology may be able to detect cancer on the atomic level.
To understand how this tool works, we need to know a little bit of chemistry; geochemist Maloney at Colorado University explains that hydrogen comes in two main isotopes, or flavors. Firstly, you have normal hydrogen, the hydrogen that bonds with Oxygen to make good ole H2O, and the lighter one of the two. Secondly, there’s deuterium, which is heavier, and is outnumbered by normal hydrogen on Earth by a ratio of about 6,420 to 1.
While hydrogen has only 1 proton and 1 electron, deuterium adds a neutron. Geologists have used this difference to analyze anything from the origin and flow of bodies of water to the temperature of the Earth when a sheet of ice in the Arctic was formed.
Ok, so what’s the big deal? Well, in the research, Maloney and her colleagues grew cultures of yeast and cultures of mouse liver cells. The idea is that cancerous cells use a process called fermentation (like some yeast cells or cancerous mouse liver cells) while normal cells mainly use respiration (like other yeast cells and healthy mouse liver cells). The fatty acids that both processes produce, Maloney’s team suspects, could have different ratios of deuterium to hydrogen, which could help differentiate two different processes, and by extension, differentiate a cancer cell from a healthy cell.
As a brief refresher from biology class, normal cells in our bodies use cellular respiration to make energy, in which it takes in sugar (mainly glucose) and oxygen, and spits out carbon dioxide and water, along with some juicy ATP, which your cells use for energy. Glycolysis, the first stage, takes the glucose and essentially breaks it in half, creating pyruvates and NADH (stuff for the rest of cellular respiration), and two pieces of that sweet, sweet ATP. This process is anaerobic, which means it does not require oxygen, but that oxygen is used in later stages of cellular respiration. This is important.
Cancer cells (and fast replicating cells), on the other hand, do a LOT of glycolysis, and then a LOT of a process called lactic acid fermentation. This process is also anaerobic, so as you can guess, it is common when there isn’t much oxygen to go around, like in your muscles cells during an intense workout. Cancer cells, however, are known to ferment sugar even when there is oxygen; this is called overflow metabolism. Lactic acid fermentation results in a lot of (shocker) lactic acid, and when it builds up in your muscle cells as waste, it creates that burning sensation. Unfortunately, lactic acids also weaken the parts of your immune system responsible for attacking cancerous cells, which makes this ‘waste’ a lot more valuable to the cancer’s survival.
In the study, the team of researchers found that respiring yeast cells had a higher ratio of deuterium to hydrogen atoms than fermenting yeast cells, even in the presence of oxygen (much like blood-supplied cancer cells). The researchers also tested this with healthy, respiring mouse hepatocytes (or liver cells) and fermenting cells within a hepatocellular carcinoma, or a liver tumor; this produced similar results.
Now while this is amazing, we don’t yet have a way to detect ratios of deuterium to hydrogen in actual live patients, but the potential is hopeful. Kopf points out that “If this isotopic signal is strong enough that you could detect it through something like a blood test, that could give you an important hint that something is off.” Detecting cancer early is invaluable to treating the disease, and thanks to Maloney, Kopf, and their team we may have a new, amazing tool in the near future to do just that.
Discovering a new “Leader Cell” by studying the process of liver regeneration
Our second story comes from Dr. Neil Henderson and his team at University of Edinburgh in Scotland, where the discovery of a new repair-cell in your liver could mean more regenerative therapies on the way.
The liver has the remarkable ability to regenerate itself. Second to only the intestines, the liver is the most regenerative organ in the body. So regenerative, in fact, that, depending on many factors, the liver can be up to 70% damaged, and within months, fully grow back (even if it may not be at full capacity). Despite this, if damage is too extensive and exceeds the abilities to regenerate (like in Acute Liver Failure, or ALF), a patient’s only option may be to have a liver transplant. However, this may change.
Dr. Henderson and his team at the Centre for Inflammation Research wanted to study how the liver regenerates naturally to potentially innovate a new curative therapy as an alternative to liver transplant. Firstly, they took human liver samples from healthy patients, patients with chronic liver disease stemming from a range of causes, and patients with ALF stemming from either Hepatitis X (not to be confused with Hepatitis A, B, C, D, or E) or APAP toxicity (overdosing on acetaminophen, more commonly known as Tylenol). They then observed the growth of hepatocytes (liver cells) in the damaged area; ALF-afflicted liver samples had more active hepatocytes than the others, prompting the researchers to focus on these samples.
Upon observation, there was a problem; while the liver did heal some of its damage by replicating cells (what’s called “cell proliferation”), it did not fully heal. To take a closer look, they sequenced genes of the liver cells, creating a pan-lineage atlas of liver cells during human regeneration. Basically, they kept track of the activity of many types of liver cells while the regeneration process took place. This is when they found a unique gene protein, ANXA2+, belonging to the new cell.
They then found this same gene expressed in a similar cell in mice and studied its functions. This cell, dubbed the “leader cell,” seemed to come out to rapidly close the wound before cell replication could repair the damage. This suggests that these leader cells prioritized preventing infection from an open wound in the liver before regrowing the liver. This discovery paves the road for new innovative therapies as an alternative to liver transplants, utilizing these novel leader cells to regenerate a liver beyond the superpowers our body already possesses. Thanks to Dr. Henderson and his team, hope is on the horizon.
Don’t forget to check out and follow The Vitals Podcast on Spotify and drop a question in the Q&A section, and you may see it in a future blog post or episode! Hate the sin, not the sinner; thank you for reading!
Let us not become weary in doing good, for at the proper time we will reap a harvest if we do not give up.
On a fateful morning at the end of September 1928, Dr. Alexander Fleming, a bacteriologist from St. Mary’s Hospital, returned to his lab in London, having taken a summer vacation in Scotland. He found his lab bench messy, but it would prove one of the greatest mistakes in history. In multiple Petri dishes grew colonies of Staphylococcus aureus (a bacteria responsible for, surprise, staph infections). Still, Dr. Fleming noticed that a mold not intended to grow in the dish had dominated the controlled environment. This mold produced chemical weapons against the bacteria, which hindered the bacteria’s growth.
It took fourteen years for Dr. Fleming to harness the antibiotic he had discovered, to refine it, and to successfully treat the first patient, a ninety-year-old woman suffering from a streptococcal infection. From then on, humanity wielded Penicillin, and other antibiotics like it, as a potent drug against diseases that would otherwise mean death: the likes of Tuberculosis, Syphilis, Tetanus, Cholera, and E. coli.
The story, however, is not over.
Antibiotics hinder or kill bacteria by targeting their vital processes — the synthesis of the cell wall (their “hard” skin), the cell membrane (their “soft” skin), proteins (their building material), and nucleic acids (their DNA) — and plenty of bacteria share these processes. Antibiotics were praised as miracle drugs to humanity, and that reputation became a double-edged sword. On one hand, antibiotics saved millions of lives, but on the other hand, antibiotics became misused. The populous began overdosing on antibiotics or not finishing their antibiotics dosage. People took expired antibiotics for illnesses, animals were fed antibiotics for their meat, and humans took antibiotics for viral infections (antibiotics do nothing against viruses).
This HEAVY misuse of antibiotics constantly applied selective pressure on virulent bacteria and presented a perfect opportunity for new bacteria to evolve. Now take this concept, multiply it over dozens of patients (who may or may not wash their hands thoroughly) in a high-traffic area — say, a city hospital — and throw in the ability of bacteria to share these drug-resistant genes. It’s all but guaranteed that a multidrug-resistant strain will eventually arise from the sickening, germ-filled ashes. Basically, humanity forced bacteria to adapt, to become resistant to our drugs. Bacterial superbugs like Tuberculosis, Gonorrhea, and Methicillin-Resistant Staphylococcus Aureus (MRSA) are already raising concern in the medical community. If nothing is done, an ultimate superbug, if you will, that is infectious, deadly, and resistant to a wide variety of antibiotics could cause the next pandemic. An ultimate superbug is the nightmare scientists are trying to avoid.
The story is still not over.
In 1915, a British microbiologist named Frederick Twort discovered the bacteriophage, a virus fine-tuned to attack bacteria. Four years later, a French-Canadian microbiologist named Felix d’Herelle came up with the concept of phage therapy: a process in which a cocktail of these phages specific to a particular bacterium is injected into the host of a bacterial infection. These microscopic assassins are so precise, so specialized that human cells and good bacteria aren’t significantly affected; the phages only kill the virulent bacteria.
As simple as that may sound, the concept didn’t gain steam back in the 20th century in favor of antibiotics. Antibiotics were better understood and much easier to mass-produce. Antibiotic treatments, in many forms, were also much easier to sell to the public than injecting literal viruses into a patient. Nonetheless, phage therapy began to receive more attention as scientists looked for effective alternatives to antibiotics. And effective, I believe, phage therapy will prove to be.
Phages are the natural nemesis of bacteria and can be found wherever bacteria are: everywhere. If bacteria mutate and gain resistance against phages (as difficult as that is, considering the many genetically unique phages that may target a few strains), they may trade away resistance to our drugs; this means phages can be used in conjunction with antibiotics as treatment. While you only receive as many antibiotics as you are given, phages are programmed to multiply using bacteria; as they kill the targeted bacteria, the phages will become without a host and stop multiplying. They’re not harmful to humans, nor are they toxic to animals (think about your pets) or the environment.
Clinical trials have shown that there is some validity to the idea. The Center for Innovative Phage Applications and Therapeutics (IPATH) at UC San Diego School of Medicine published data from ten cases of phage therapy (through intravenous injection, or through the veins) to treat multidrug-resistant bacterial infections. Seven out of the ten cases had a successful outcome; there is hope, but many obstacles remain.
There is no way to mass-produce phages as of now. Definitive doses accounting for various factors are yet to be flushed out. Finding exact phages to target specific bacteria is tricky. The human immune system may react negatively to introducing, again, literal viruses to the body. Not all phages make for suitable treatments, and some bacterial strains may not have a phage associated with them at all.
The discovery of antibiotics still stands as one of the greatest advances in medical history; one of many monumental innovations in medicine like anesthesia, vaccination, insulin, and organ transplants. Phage therapy is the next weapon to be perfected and refined in this arms race against illness, ushering a new era of precision medicine and a healthier humanity.
The following is an essay I wrote for English class in response to a prompt that read something along the lines of, “Write a personal narrative of an experience in your life, show what you learned, and show how you have grown.” If you’re looking for essays to read, this is a good example. Enjoy!
“…Chauncey Taylor!” the pastor called, prompting me to walk up the aisle and shake the imposing man’s hand. The primary donor, a motherly woman sitting in the front row, smiled and clapped with the congregation as I stepped onto the altar. It all felt so surreal; the pastor introduced me and my situation, but I had never had so much attention and weight on my shoulders as I did that day on the altar..
“…put your hands together for brother Chauncey!” the pastor concluded. A few brief seconds of applause erupted through the sanctuary as the microphone fell to my hand. I realized it was now my turn, and as I brought the microphone to my mouth, the sanctuary instantly fell silent. How did I get here?
***
Two months prior, an email from my mother stood out in my inbox; she rarely uses her email, so it piqued my curiosity. Clicking it, I saw that she had replied to an email sent two years ago; I had just become eligible for a brotherhood I took an interest in, and my mother resurfaced the email. A few more replies later, I am suddenly tasked with writing an essay and recording a short introduction video around the same time sophomores shift their focus to final exams for the year.
At first, I found this extremely inconvenient, but after looking over the email thread once more, my mother had emailed back and forth with the brotherhood about a Harvard Medical School summer program. The buzzword caught my eye and convinced me to throw my hat in. I stressed myself out and stretched myself thin between school, my obligations as a big brother, and these new responsibilities. My mental health was not perfect, to begin with; this new burden made it worse, and it showed in school and at home. Nonetheless, I pressed forward. One heartwarming essay, an extensively rehearsed video, and a congratulatory email later, and I am inducted as a scholar at Greeks United International.
A representative from GUI reached out to me a month later regarding the Harvard program. My heart fluttered reading the title, only to sink as the email told me I had less than a week to fulfill the requirements, from health insurance to two more short essays. The ensuing days were, yet again, a mixture of a healthy dose of chaos, plenty of stress, and juggling priorities, but I could already see the grand, marble Harvard Medical School sign in my future. It would all be worth it.
It is important not to sacrifice your mental health for your work.
After practically hounding my guidance counselor to finish their recommendation and throwing together my high school transcript, I submitted my application and held my breath for the next week.
They accepted me! What’s more, a friend, a part of my church’s leadership, offered to pay for most of the acceptance fee on the church’s behalf! It would, however, come at a cost; the grant did not cover food and lodging.
Fortunately, the representative from GUI invited me to speak to the congregation as a general introduction to how I operate academically and what I see in my future. They gave me a month’s notice to prepare for the most important and influential five minutes of my adolescent life.
Within the first two days of this notice, I had a speech written and revised. I forwarded it to my parents, friends, teachers, and anyone else I knew. I even let ChatGPT give its input. For the following three weeks, I balanced studying for finals and rehearsing for the thrilling yet foreboding oratory, the date slowly creeping closer day by day. Two weeks turned into one week, which shortened to a few days. One morning, I woke up and realized that the presentation I had prepared was only a day away.
Inevitably, that Sunday morning came around. The morning replays in my head all the time; I woke up early, exhausted and slightly burnt out. I prepared for the day and dressed in a formal polo shirt with khakis; I took far too much time pondering this simple appearance, only to forget to iron the pants I settled on. It only added to the tension, but now wasn’t the time to fill my head with thoughts of dread. One moment, I twiddled my thumbs, mumbling my speech to myself on the car ride to church. The next moment, I stood alone on the altar with a microphone in my hand and all eyes on me.
And so, I started.
Sometimes, public speaking works best when you feed off the audience.
I introduced myself, I recited Proverbs 22:6, “Train up a child in the way he should go; even when he is old he will not depart from it,” and I repeated a common slogan in our church, “Know who we are in Christ, Embrace who we are in Christ, and Walk Out who Christ says we are.” This simple start helped lead me into the rest of my speech, and strangely, miraculously, the words began to flow, to come to me. Much of what I said came from my script, but I ventured off the beaten path just a little to pick a few special roses for my audience, roses I could have never bought at any bouquet shop. I found comfort on the altar as I paced back and forth across it. I cracked a joke, and the audience laughed; I made a great point, and they filled the sanctuary with applause. Any anxiety I had, any doubts or worries that lingered in my mind seemed to melt away; my confidence came from the congregation, and I finished before I knew it.
In hindsight, I realized how stressed I was beforehand and how much I stumbled over myself, yet I still gave the speech. I still found the words, I still summoned the courage to speak despite my shortcomings, and I never would have thought the worries and doubts that were so human could be behind something so spectacular. Countless times, I find myself pulling my abilities thin, often sacrificing my health to “get the job done.” I constantly push myself to make sure what I produce is purposeful and substantial; most of the time, my ambition can be beneficial, and it helps me strive for greatness. Other times, however, my blind ambition can often drive me to chase perfection, some unrealistic goal, the golden fruit far too high to reach.
This experience helped me learn that I’m human and that it’s okay to tend to my emotions and health. I learned that stretching myself thin does no good for anyone; had I properly managed my mental health and avoided burnout, my speech may have been ten times better. Since this milestone in my life, I have kept myself from sacrificing my health for results, and I feel that it has helped me in more ways than one.
“Thank you,” I crescendoed. “Again, I’m Chauncey Taylor! Remember that name!” The standing ovation echoed in my ears. I spotted my dad recording, smiling with pride beside my little sister. A week later, I learned I had raised over $3,000 for my trip to Harvard Medical School. This speech still stands as my most significant accomplishment to this day, but most importantly, I learned that it’s better to leave the roboting to the robots.
So we fix our eyes not on what is seen, but on what is unseen, since what is seen is temporary, but what is unseen is eternal.
