Sunday, September 27, 2015

Bacteria, Botulism, and Beauty

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By Talya Klinger, MSS Intern

The molecular structure of botulinum toxin
What do foodborne illnesses, neck dystonia treatments, and celebrities’ beauty regimens have in common? Clostridium botulinum, baratii, and other species of Clostridium bacteria produce all of the above and more. These seemingly innocuous, rod-shaped bacteria, commonly found in soil and in the intestinal tracts of fish and mammals, produce one of the most deadly biological substances: botulinum toxin, a neurotoxin that intercepts neurotransmitters and paralyzes muscles in the disease known as botulism. Nonetheless, botulinum toxin isn’t all bad: this chemical not only protects the bacteria from intense heat and high acidity, but it makes for an effective treatment for medical conditions as wide-ranging as muscle spasms, chronic migraines, and, yes, wrinkles. 


C. botulinum
Clostridium botulinum and similar bacteria can make their way into the human body in a number of ways. Wounds infected with Clostridium botulinum or spores ingested by infants can lead to the rare but serious disease of botulism, as can accidental overdoses of medicinal or cosmetic botulinum toxin. Botulism is often foodborne, usually contracted by infants from honey or by adults from improperly home-canned foods and unrefrigerated herb-infused oils. Regardless of where any case of botulism comes from, it causes muscle paralysis, which can manifest as blurred vision, dry mouth, and muscle weakness in adults or lethargy and constipation in infants. These are only early warning signs for an illness that, if left untreated, can paralyze a patient’s respiratory muscles to the point of asphyxiation. Although 95-97% of botulism patients receive treatment and survive, they often require months of intensive care and suffer years of muscle weakness, fatigue, and shortness of breath.

So how does the neurotoxin that makes botulism so deadly work? Clostridium bacteria produce several protein compounds with similar structures and molecular weights, consisting of two chains of amino acids—one small and one large. These two amino acid chains are linked together by a covalent bond between two sulfur atoms, one in each chain. The botulinum toxin proteins bind to nerve endings where they join muscles, blocking the neurotransmitter acetylcholine, which ordinarily causes muscle contractions. This blockage is permanent, paralyzing the muscle until a new nerve ending forms a synaptic connection with it. Because the process of forming new neuromuscular junctions takes at least 2 or 3 months, the affected muscle will often atrophy in the meantime, causing the long-term side effects that plague botulism survivors.

Ironically, the very mechanisms that make botulinum toxin so dangerous give it a wide range of beneficial medical applications. When botulinum toxin is administered in small, controlled doses, its muscle-contraction preventing effects make it a viable treatment for neck dystonia, sustained involuntary eyelid closure, chronic migraines, neurogenic bladder dysfunction, and other conditions caused by involuntary muscle movements. In popular culture and tabloid media, Botox’s serious medical applications are often overshadowed by its cosmetic notoriety: smoothing out wrinkles. Cosmetic Botox inhibits the neuromuscular activity that leads to wrinkles, relaxing the surrounding skin. Seeming to reverse one of the telltale signs of aging may have given botulinum toxin its Hollywood appeal, but its wide ranging pharmaceutical uses are what continue to fascinate research scientists.

In a nutshell, the molecule botulinum toxin is a toxic protein made by clostridium botulinum bacteria. In measured amounts, the toxic protein is marketed as Botox for pharmaceutical uses. When uncontrolled doses of the bacteria are ingested, however, Clostridium botulinum can result in deadly cases of muscle paralysis called botulism. 

 If you are intrigued by the terrible beauty of such a versatile molecule as botulinum toxin, come to Marin Science Seminar on September 30th, at Terra Linda High School, 320 Nova Albion Way, in Room 207 from 7:30 to 8:30 pm, when bioanalysis and pharmacology expert Dr. Erik Foehr will discuss his research on botulinum toxin.

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Saturday, September 12, 2015

An Interview With Dr. Erik Foehr


By Zack Griggy, MSS Intern, San Marin High School, Novato

          In today's world, infectious disease remains a deadly concern to humanity. Some of these diseases include anthrax, Venezuelian equine encephalitis, bubonic plague, MERS, Eastern equine encephalitis, and, of course, botulism. Botulism is a disease that can cause paralysis and even death, but what makes botulism so different from the rest of these diseases is that the substance that causes it, botulinum toxin, is widely marketed as a beauty product under the name Botox. Dr. Erik Foehr, an expert in the fields of bioanalysis, immunogenicity risk assessment, and drug development, is currently investigating the toxin and how the body responds to it. Attend his presentation at Terra Linda High School, 320 Nova Albion Way, in Room 207 from 7:30 to 8:30 pm on September 30th.



In order to gain a little more insight before his talk, we interviewed Dr. Foehr about his work and research.


1. What drew you into the fields of pharmacology and bioanalysis?

I have always enjoyed learning about biology and how living things work.  After high school at Drake, I went to UC Davis and studied genetics and biochemistry.  I eventually worked in the biotechnology industry and specialized in pharmacology and bioanalysis.

 2. What have you studied in the past and how did this lead to your study on botulinum toxin?

I studied cell biology and how cells signal and function. I also spent many years studying immunology.  In my current job I study how botulinum toxin works and test if people develop antibodies to the toxin.

 
3. How is botulinum toxin used in beauty products? How are dangers minimized by these products?

Its a bit crazy to think something so dangerous can be used as a beauty product (it removes wrinkles).  The trick is to use a tiny amount and inject it at the site of the wrinkle. The toxin inhibits the neuro-muscular activity so that the skin looks "relaxed". They are finding other more medically relevant uses of the toxin.

 4. What do you enjoy the most about your work? What do you enjoy the least?

I enjoy learning about the huge number of experimental new drugs being developed for unmet medical needs and helping to study them. Sometimes I would like to spend more time "thinking" and less time "doing".

 5. Do you have any advice for high school students who aspire to be pharmacologists?

Study what interests you and be prepared to be a life-time learner. Science and technology move really fast and you need to adapt and learn on the go. Don't get replaced by robots!


Join us Wednesday, September 30th, at Terra Linda High School, 320 Nova Albion Way, in Room 207 from 7:30 to 8:30 to hear Dr. Foehr talk about his work and his study on botulinum toxin and other lethal diseases. 

Tuesday, September 8, 2015

Chemosynthesis in the Deep Sea

Chemosynthesis In the Deep Sea
by Jane Casto, MSS Intern, Terra Linda High School
     
          The deep sea- where cold, stable pressures and darkness rule. Within that darkness lies life; a broad spectrum of biodiversity. The most fascinating thing about the deep sea, however, lays within what goes against lifeforms on land. 
          On land, plants and animals alike require some form of energy. The same is true in the deep sea, but one thing, particularly about plants, is quite different. Photosynthesis, the process plants use to turn sunlight into usable energy through chlorophyll, is almost always the method that plants use to get said energy. However, in the deep sea, quite a difference can be seen with that process.
          One of the reasons as to why deep sea ecosystems, such as hydrothermal vents, do not use the process of photosynthesis is obvious. Little sunlight reaches that far down into the ocean. With that in mind, however, the question presents itself: how do these ecosystems get their energy?
          Jenna Judge has studied just that. Her research has been following Marine Biology, specifically the deep sea and, our answer, chemosynthesis. Chemosynthesis is the process in which energy is obtained by reactions of inorganic chemicals, occurring within bacteria and other living organisms. 


          "Chemosynthesis also seems to be fueling ecosystems at organic substrates, such as whale falls and wood falls." Jenna said during her presentation, Patterns of Specialization in the Deep Sea, "We found that rather than sunlight fueling this reaction, it's reduced molecules such as sulfide, and in other cases, methane, than can fuel these microbial metabolisms." 
          According to wiseGEEK.org, the process relies on oxidation, or redox reactions. Organisms, namely bacteria and those that belong to the kingdom archea, use chemosynthesis to manufacture food. This food is used as a carbohydrate, made of carbon dioxide and water, rendering it usable for the bacteria just as a carbohydrate would be usable to us. 
          While the deep sea is one of the most extreme examples of chemosynthesis, believe it or not, chemosynthesis is also found on land. The key is that chemosynthesis occurs where sunlight is not present. Therefore it can occur in a variety of places above land, i.e. in soil, in the intestines of mammals, and in petroleum deposits. In fact, some scientists believe that due to the tendency of chemosynthesis to take place in extreme environments, it may feature prominently on other planets depending on weather patterns. 
          The deep sea has many unexplored aspects. It is nice to know that some things are no longer a mystery, and it is also exciting to think about the fact that it is not yet fully explored, leaving room for ventures for years to come.

More on the deep sea at the first seminar of the season, with Jenna Judge.
Wednesday, September 9th, 2015
7:30 - 8:30 pm
Terra Linda High School, San Rafael
Room 207