Seal flu, a productive Christmas, and reading clinical trials
|Katherine Ellen Foley||Dec 31, 2019|| 1|
Dec. 31, 2019
Hello friend! Welcome to Scrap Facts.
I'm a reporter covering health and science with insatiable curiosity. I love everything I learn, not all of which gets its own story. Each week, I'll bring you some of my favorite facts that I picked up on the job or while out living life.
It’s the last issue of the year! Scrap Facts is a labor of love. If you’ve loved (or even moderately enjoyed) all the Scrap Facts throughout 2019, please consider tipping me through my Venmo. All donations go to my chocolate/granny smith apple fund.
One of the major flu strains this year is likely harbored by…harbor seals.
Found while reporting: The flu is worse this holiday season than it was last year.
I’d like to add “flu season” to the list of life’s certainties.
Every year flu season rolls around (from about October through March for us in the northern hemisphere, the opposite time of year for those in the southern hemisphere) it’s different. It seems to be more active than usual for this time of year, in part because a strain of the virus called influenza B is more prevalent this year. Normally, influenza B only pops up at the end of the year; influenza A is the star of the show.
For most people, this is a negligible difference: both strains make us sick with the same nasty symptoms. For virologists, the difference is in the proteins that make up the core of the virus. For public health experts, the difference is in the trouble these viruses cause: Influenza A tends to be the one that causes pandemics, whereas influenza B can lead to mere seasonal epidemics.
For seals, though, the difference is that one can make them sick. Influenza B antibodies have been found in both harbor and grey seals. Because antibodies are the result of prior infections (or vaccines!), it means seals have encountered the virus before. They could also be a reservoir for the virus—meaning they could pass a version of it to us—just like some birds or pigs could spread versions of influenza A to us.
There are influenza C viruses, which cause less severe illness, and D viruses, which only trouble cows—not people.
If you haven’t gotten a flu shot, please consider getting one! It’s not too late, and even if it doesn’t protect you from the flu entirely, it can make it easier to get through.
One of the biggest discoveries in longevity research happened on Christmas Day.
Found while reporting: 10 years after the Nobel Prize, telomeres are still a murky lead in longevity research.
This Christmas Day (Dec. 25), I spent the day gorging myself on Chinese food and playing pool. Thirty-five years ago in 1984, Carol Greider, then a graduate student in biology, had a much more productive holiday. She discovered the enzyme telomerase, and won the Nobel prize for it in 2009. At the time, she was 23 years old.
Telomerase is the enzyme that builds up telomeres—which are the part of our chromosomes that act like a little genetic hourglass. Every time our cells divide, our telomeres shorten. When they get too short, our cells stop dividing, and they die. It’s a mechanism of aging—although there’s no one source of aging.
Longevity researchers have jumped on telomeres and telomerase as the one way to stop, or maybe even reverse aging. If we can just get cells to rebuild their telomeres, maybe cells can keep dividing.
Alas, there’s one major problem. Telomerase is only in a handful of healthy cells (blood, sperm/egg, and some GI tract), but it shows up in 95% of cancer cells. Playing with telomerase, therefore, runs the risk of causing cancer.
Instead, most longevity researchers have switched their thinking: They’re on the hunt for all the ways that telomeres shorten outside of regular cell division.
Bonus fact: Most enzymes, which help a particular chemical reaction occur, are usually just giant proteins. Telomerase, though, has a special genetic material component called RNA—making it more biologically impressive.
A note on healthy skepticism with clinical trials.
Soon, in the early new year, the drug company Biogen will likely file for approval for their Alzheimer’s-slowing drug, aducanumab. It’s an amyloid-protein antibody, given through monthly IVs to patients with mild Alzheimer’s disease, and it seems to clear out amyloid while slightly improving cognitive function.
It’s huge news: There hasn’t been a new drug for Alzheimer’s in over a decade, and lots of desperate people are likely willing to pay anything for a new hope against the disease. And even for a drug to get approved at all is a moderate deal—only about 13.8% of drugs that go through the clinical trial process make it to market.
But just because a drug is approved doesn’t mean it’ll work.
The US Food and Drug Administration requires drug companies to go through three clinical trials—meaning, in people. The first looks at whether the drug is safe in healthy people. They’re small, and they pay. The second is a little bigger, and looks at whether the drug actually works, and the third, which involves thousands of people, sees if it’s better than existing treatments, and what side effects may occur.
The aducanumab trials—two identical trials—involved nearly 3,000 people with Alzheimer’s. That may seem like a lot, but in the grand scheme of things it isn’t: the people who participate in clinical trials are usually homogenous. Alzheimer’s disease—or any condition, for that matter—is very diverse in who it affects, and how it manifests in the body and how it needs to be treated. Notably, these trials were also not successful at first; Biogen originally discontinued the clinical trials because it seemed like it wasn’t working. Not confidence-inspiring.
If (when) Biogen submits aducanumab to be approved, the FDA will review how it did the trials, and the results, and then decide whether or not it should be approved. I say all of this not to say the drug is bad—it’s definitely inspiring—but it’s not wise to put all your hopes on it, or any drug.
Animal(s) of the issue: the 412 new species discovered this year
Scientists at the Natural History Museum in London added over 400 new species of plants and animals to the known list this year. It was a lot of invertebrates and beetles, and a handful of moths and butterflies, and a couple snakes. It just goes to show that we still don’t know all that’s out there.
Sadly, though, we’ll likely never know all the creatures we share the planet with. Because of human activity that leads to animal extinction, “we are losing species faster than we can discover them,” Tim Littlewood, the Museum's Executive Director of Science, said in a statement.
Did you know that the creators of the Pokémon universe have noticed this trend too? Corsola, a coral-like creature, has been bleached out to a ghost of its former self—the same fate as many real corals as a result of ocean acidification.
Corsola—before and after. Image credit to The Pokémon Company.
My colleague Daniel Wolfe made an awesome quiz that tests your ability to pick out Pokémon from actual species discovered this year. It’s fun! And cool that the stark realities of climate change are reflected in Pokémon.
Stuff I learned from others:
Ben and Jerry’s may not be the cow-friendly ice cream we’ve always thought it was. Armadillos help scientists study the differences in identical twins. Kelly Clarkson is coming for Mariah Carey’s Christmas dominance. Holland wants you to call it “the Netherlands” now.
If you love Scrap Facts, consider hitting the “like” button at the bottom of this page, or sending it to a friend. You can also send your own scrap facts to firstname.lastname@example.org to be featured in future editions. Wanna keep in touch outside of this newsletter? Follow me on Twitter and Instagram.
Top image by E. Y. Smith, headshot drawing by Richard Howard.