Science Communication Advice from Alan Alda

 

This one is for the scientists!

I saw Alan Alda speak this evening at UCSD about “Helping the public get beyond a blind date with science.” He made a case for telling your science story in personal, simple, engaging language. He also told us about the efforts at the Center for Communicating Science at Stony Brook University to prepare graduate students with communication tools. He was funny and grandfatherly and such a good presenter himself. I’d like to share the insights I gained about getting people to listen to and understand you, especially with science.

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I got there late, because UCSD parking sucks, so this photo is from quite far away.

Be conversational, not lecture-y

One of Alda’s first important points was that scientists communicate differently when they are speaking one-on-one with someone instead of presenting a lecture. It is not only the jargon-y fanciness of the words that differs, but the speaker’s tone will tend to be colder and less personal in lecture mode. And when scientists speak about science, we often fall into lecture mode out of habit.

He uses the analogy of falling in love to explain how we can engage the public. Right now science is a “blind date” to the public– an unfamiliar person in the room making them uncomfortable. Alda says “there are three parts to falling in love – and if you haven’t heard of them before, it’s because I made them up,” and these are 1) attraction, 2) infatuation, and 3) commitment.  As an analogy, these stages to love translate to: 1) first impressions when you are communicating, such as welcoming body language, a warm tone, and personal language; 2) memorability, which happens when your audience has an emotional response (any emotional response helps someone to remember that moment); 3) commitment, and I didn’t catch this one from Alda, but I think commitment means your audience will remember scientists to be trustworthy, comfortable sources for information and discussion.

Be a story-teller                                

Tonight Alda told us a lot of stories. Because of this style, we laughed and followed each point he made easily and willingly. And one of his main points was that people like to hear stories.

What makes a good story? This is definitely not something we learn as scientists, except to make “a story” out of our data so it fits into the bigger picture. But he made a point to show that it simply involves an objective (that matters) and the obstacles that must be faced to attain that objective. Alda’s example used a woman from the audience, and she had to carry an overfilled glass of water across the stage without spilling (or her village would die). Our objective would seem to be the significance section of our proposals, so we already have that part floating in our grant-writing brains, and it mustn’t be left out of our public communications. The names of the proteins can be. And words longer than three syllables.

Another important thing about stories is the emotional element, as I mentioned, since people remember things when they have an emotional response to them. Use emotion words. Socialization is our greatest strength as a species, and so much can be gained from plain communication with each other.

 Where does communicating science fit into science?

This issue seems like an ongoing discussion.

Why do we need to be better at telling the public about our science? For one, the general public contributes to science through taxes and thus it is a voter’s issue. Informed voters are crucial to a better society. Obviously. Two, we want them to trust us when we recommend things like vaccines. Three, we should be smart enough to recognize when we need to improve ourselves, eh?

The public aside, Alda brought up a good point about scientists from different fields not clearly communicating with each other. This language barrier is no secret among scientists, as there is a sense of pride among at least the younger scientists that may prevent asking about jargon clarification instead of big picture questions. I’ll admit I avoid neuroscience talks.

The moral of this story is that we need to practice talking about science as people and not scientists. It’s not easy, which is why Alda has created an institute to teach it to grad students, while they are still being molded into scientists. I’ve heard a number of other scientists say, ”why should we bother explaining things to the public when we have important things to do in lab?” But it is more about being prepared for interactions with a lay-audience, and like I said, being able to communicate clearly with other scientists. Just think of the ideas that could come out of increased understanding among different science fields! Increased understanding of what scientists do, how they do it, leading to increased interest by the next generations, and to top it off, better scientific ideas flowing between scientists? Why wouldn’t we want better science communication?

 

A recent interview with Alan Alda: http://www.theatlantic.com/education/archive/2015/01/science-in-the-words-of-alan-alda/384218/

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Reasons I love the movie Contact

….

I first saw the movie when it came out in 1997, and I was in 8th grade. I don’t know if it was my favorite movie immediately, but it is now, and I think it was when I started to imagine myself as a scientist that I really clung to the things in this movie. These were the aspects that stood out…

I. Ellie Arroway was the type of woman I wanted to be when I grew up. She’s independent and driven.

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II. She had THIS guy in her bed, and the next morning she’s all like alright, I’ve got work to do, later.

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III. She’s got taste.

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“Uh, do you know where I can find like a really great dress?” Ellie Arroway

IV. She is a badass confident woman who can hold her own.

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“You wanna hear something really nutty? I heard of a couple guys who wanna build something called an “airplane,” you know you get people to go in, and fly around like birds, it’s ridiculous, right? And what about breaking the sound barrier, or rockets to the moon, or atomic energy, or a mission to Mars? Science fiction, right? Look, all I’m asking, is for you to just have the tiniest bit of vision. You know, to just sit back for one minute and look at the big picture. To take a chance on something that just might end up being the most profoundly impactful moment for humanity, for the history… of history.” Ellie Arroway

V. The beauty of the visuals and the story itself

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“You’re capable of such beautiful dreams, and such horrible nightmares. You feel so lost, so cut off, so alone, only you’re not. See, in all our searching, the only thing we’ve found that makes the emptiness bearable, is each other.” Alien

Published! Role of a Nuclear Localization Signal … in BK Polyomavirus Nuclear Entry

My second research paper from my graduate school lab finally came out, and I would like to try to summarize it for you here, in layman’s terms and with cartoons instead of figures because I’m not sure how copyrights work and I don’t feel like searching for old data. The headings are taken directly from the paper.

Introduction

In my first paper, I showed evidence that BK virus travels from the cellular compartment called the ER into the fluidy part called the cytosol on its trip towards the nucleus within a cell. Another big question in the field is how the virus enters the nucleus. The nucleus of the cell contains our DNA, so obviously it doesn’t let just any protein-sized object into it!

So as a follow up to my previous paper, I set out to determine whether the virus gets into the nucleus from the cytosol using the pathway that other nuclear proteins use, where a specialized import protein recognizes a “signal sequence” on the nuclear protein that signals the import protein to send it into the nucleus. This was the hypothesis on which I based my experiments. It is summarized here in this figure below.

????????????????Figure: After coming out of the ER, the virus (in red) uses a signal on one of its structural proteins to interact with nuclear-import proteins (in green) to enter the nucleus (through the Pore):

Lysine 319 on VP2 and Lysine 200 on VP3 are critical for nuclear localization of the minor capsid proteins.

The first thing that we had to do was to look for the nuclear localization signal on the virus. Based on what the signal looks like on other proteins, we hypothesized that a couple of amino acids on the minor structural protein provided the signal. So we mutated one specific amino acid in that area of the protein and looked at the protein within a cell.

We found that normally the protein goes to the nucleus. However, with the mutation, the protein remains outside of it. (We determined this by microscopy and fluorescently labeling the protein). This suggests that the amino acid we mutated was needed for signaling nuclear localization.

????????????????The VP2/3 NLS is important for entry in RPTE cells

The more important question about this nuclear localization signal is whether it is needed when it is part of the whole virus capsid, and not just a lone protein. So, we made virus containing this mutation in its minor capsid structural protein. Then, we infected cells with this mutant virus to see if it can infect cells as well as the normal (“wild-type”) virus. We found that it could not infect the cells as well as the wild-type virus. We could deduce from this finding that the one amino acid in that one protein was important for… well, something… during the infection (although we hypothesize that it is needed in nuclear entry, this data alone doesn’t give us conclusive evidence… so, next experiment).

????????????Importin β – mediated nuclear import is involved during infection

The other way we can look at this “pathway” is from the other side of the picture – does the import protein that is floating around in the cell, looking for nuclear localization signals, play a role in infection? This protein is call “importin” – because it imports proteins into the nucleus, clever right?

We looked at this question in two ways, the first of which was to take away that specific importin protein in a process that we call a knock-down. We introduce a RNA molecule into the cells that will cause the importin to no longer be made. Then, we infect those cells with the virus, and compare the infection with cells that have not had the protein knocked down. What we found was that without importin, the cells were not as easily infected. Again, this tells us that importin was important for something during the infection.

Model KDThe second way we tested this pathway was to use an inhibitor called ivermectin that targets importin’s function. This chemical gets in the way when importin tries to interact with its target – in this case, the virus. So we treated cells with ivermectin, and then infected with virus (and compared to what? You guessed it, cells that were not treated with ivermectin). What we saw was that the cells treated with ivermectin did not become infected as easily, implying that infection needed something that the ivermectin was blocking.

???????????????Discussion

In this paper, combined with my previous work, I identified components of a kidney cell that BK virus uses to cause infection – specifically, the nuclear import protein importin (and likely its helper proteins).

Are there alternative interpretations to these conclusions? Like a court case, we base a lot of things on the best interpretation of the evidence – are there possibilities that we haven’t considered? It is likely – things that scientists haven’t discovered yet about the cell, for example. It is also possible that our interpretation is missing some details. That is why we present the data, along with our methods and conclusions, so that other members of the scientific community can evaluate it and use it to make other hypotheses to reach our end goal of helping sick people get better.

If each of these methods blocked infection in the cells, can’t we use them now to block infection in people? In general we are able to manipulate the cells easily because they are in a plate. In a person, there are so many different types of cells, and a lot of those cells would probably need the importin protein to keep working to keep that person alive. The same is true for the treatment with ivermectin – it is actually very toxic, and although it prevents the cells in the plate from being infected, after a couple days the cells would die anyway from the treatment.

Progress depends on what has already been done, and ideas that have been presented, to support and invoke new ideas and hypotheses about how nature works. My work on how BK virus gets to a cell’s nucleus has brought us one step closer to treatment of BK virus infection. Since other viruses may use the same pathway, if a drug is discovered that targets BK virus, it may also be useful for those other viruses. It will be so exciting to see what is discovered next!

Sunshine and Adenovirus

A new lab, with a lot to learn.
I started working in my postdoc lab at the beginning of June, and now I’m finally feeling settled enough to start doing things other than reading research papers.  Ok, admittedly I started a Muay Thai class a month ago (because I’m badass) and I’ve done some painting (because I’m not badass I’m actually an artsy nerdy skinny girl), but I’ve found that creative and physical outlets are extremely important for my mental health as a scientist. Research is so mentally exhausting sometimes, and life is all about balance, right? Especially when you don’t have any friends and the other postdocs are busy with babies or something.
Now that I’ve gotten a better grasp of my new field and the directions of my project, I thought I’d tell you about it.
Adenovirus!
My lab studies adenovirus, which is actually not very different from the virus I worked on in my last lab, polyomavirus. There are different categories of viruses, and these two are small, nonenveloped, DNA viruses – meaning, they have a tiny DNA genome (instead of RNA), and this genome is contained inside a polyhedral shaped “capsid” shell made up of just a few different proteins.

I liked the simplicity of this diagram. 
Why would anyone care about adenoviruses?
Well, adenoviruses are important to understand for a number of reasons, the first one being that they can cause illnesses. A common problem they cause is respiratory infection in children, and a different strain of the virus can cause a bad form of pink eye. And like every other pathogen, they can cause a problem for anyone who is immunosuppressed.
Another interesting thing about adenoviruses is that they can be manipulated and used in a helpful way, for gene therapy (where someone with a genetic disease would be treated with virus that had been altered to carry a functional version of the gene causing the disease).
A third interesting way that adenovirus might be helpful is that the virus can be used to kill cancer cells. The idea is that the virus has to selectively kill the cancer cells but not healthy cells, without first being taken out by the immune system.
A virus that kills cancer: the cure that’s waiting in the cold  (I just wanted a simple article about the therapy but this piece gives an interesting story)
What am I working on?
My goal in the lab is to get a better idea of the disassembly mechanism of adenovirus. What does that mean? Well, when the virus finds a cell, and then gets inside, its main goal is to replicate and make new viruses. In order to do that, it needs to get its DNA inside the nucleus of the cell. But if you remember, the virus DNA is protected inside a layer of proteins called the capsid, so the virus capsid has to break apart somehow to free the virus DNA. This is not a simple task, because the whole point of the virus capsid is to be very strong and stable so that it can travel from one person to another during transmission and then through their body. So, viruses have evolved to interact with specific features inside the cell to trigger “loosening” of the capsid and subsequent disassembly steps.
Why is it important to understand the virus disassembly process?
Understanding the basic steps of a virus’s life cycle – how it gets into the cell, comes apart, and gets its DNA into the nucleus to replicate – is important for a lot of reasons, even if it may not seem immediately “translatable” to the clinic. One main reason is for discovery of anti-viral drugs, because these are often designed to specifically stop a step in the lifecycle such as disassembly. If the virus capsid can’t come apart, then the virus can’t infect the cell. In terms of gene therapy or cancer therapy, understanding how the virus interacts with the cell is important so we can manipulate the immune response and/or figure out how we can target the therapeutic-virus to specific cells in the body.
Well I think this general overview is good enough for now. I don’t like overwhelming anyone. Including myself. Back to the lab bench! Today I’m looking at how the interactions of adenovirus with its receptor proteins impact its stability, which you can actually look at by just mixing them together….

Sorry, I’ve been busy, but I wanted to post an update at least.

I successfully defended my PhD!

I got a gold star. 😉

I have a job!
I will be doing a post-doc with Glen Nemerow at the Scripps Research Institute in La Jolla, CA. Working on adenovirus.

Look how cute it is! It wants a hug.

More updates and sciencey posts soon, I promise.

My Dissertation (Intracellular trafficking of BK Virus: from the ER to the nucleus)


So, I set a date to do my thesis defense, on December 13. This means I have until the end of November to submit my dissertation to my committee… which means, I should be working on it right now. Instead, I thought I would try to explain my work here where I don’t have to use big words all the time.

The BK Virus (Signficance)

The lab that I work in does research on BK Polyomavirus.The BK does not stand for anything. Would it really matter if it did? Call it the Burger King virus like my family does. Anyway, “BK” is a virus that is actually already inside 90% of people because we pick it up when we are dirty kids. But that doesn’t matter, because healthy people aren’t really affected by the virus and it just hangs out quietly throughout your life. That means it’s actually very good at being a virus because it is able to quietly spread through the population without making a mess… that’s a conversation for another time, though.

Why do we study this virus? We get funding to study this virus because it can cause problems for people on immunosuppression, especially people with kidney transplants. When the immune system is taken out of the picture, the virus gets out of control replicating in the kidney cells and can basically destroy the new kidney.

Importantly, we don’t have any anti-viral treatments for BK. This is partly because there a lot things we do not know about how the virus works. That’s where I come in! And other researchers.

My Research (Introduction)

The way that anti-virals work is they usually block a process in the virus life cycle.  There are a lot of different things that need to be known about cells and the virus and how they interact if you are going to make a drug that gets in the way. So, basically my goal is to understand how the BK virus interacts with the cells. I am doing that by figuring out how it travels (or “traffics”) through the cell. I am not looking specifically for a cure for BK infection, but I am learning all about how the virus uses and messes up normal cell biology. Then, someone else can use that information to make informed decisions about what drugs might stop BK.

How do we figure this stuff out? (Materials and Methods)

Basically, I work with human kidney cells in a petri dish, and I infect them with virus. All you have to do is put some pure virus on top of the cells, they will become infected. I can tell they are infected by looking for a certain virus protein after a day or two. So, to answer my question of what the virus interacts with inside the cell, the main way to do that is to take away certain things in the cell, and see whether they can still be infected, and what is happening if they can’t be infected. Interestingly, the cell can still function pretty well without specific proteins or pathways.

We can take away cellular functions in a few different ways. The method I’ve used most often is I treat the cells with a drug that specifically stops certain proteins and cellular machinery from working. These types of drugs are often only used in research to help figure things out. They are super convenient.

What did I find? (Results)

Do you remember high school cell biology? What I found is that BK travels from the outside of the cell, into the endoplasmic reticulum (the ER), then into the cytosol by using something call the proteasome and ER-associated degradation pathway, and gets into the nucleus by using the nuclear pore. I’ve illustrated it below (obviously using MS Paint).

At this point you might be like, gosh who cares?! This is boring. Well, shut up. It’s super cool that a virus can go from outside your body to inside your body and then inside your cells and then travel through the cell and disassemble and put its own DNA into the nucleus of your cells and replicate. Watch the Battlefield Cell video!

What does all this work I did contribute to science? (Discussion)

The goal of scientific research is obviously to contribute to science by providing information that was not known before. My research hasn’t changed the world (yet) because we had hypothesized that these things were true based on work that had been done with similar viruses, and then gave evidence that they were true. But that’s what a lot of science involves – supporting hypotheses that are out there but haven’t been given much “convincing” evidence yet. My hard work has contributed to the field of virus research because it has provided data that did not exist before.

What helped me finish grad school? (Acknowledgments)

I would like to acknowledge these things that have been with me through these past five years:
anti-anxiety meds, alcohol, cardio workouts, cookies, things that remind me why I love science, beer, friends that make me laugh, realizing that I can still be called a scientist after failing, people who tell me I’m smart.

How to work with Ebola virus.

I have a thing for science, obviously, but viruses are my ultimate love. It’s the field in which I am working toward my PhD (and hopefully will receive in the next few months). Related to this, I follow an awesome virology blog and podcast put on by Dr. Vincent Racaniello. I highly recommend these resources because they are meant to be useful for non-scientists.

Anyway, I just wanted to share a cool thing they did, which was to create a documentary about a biosafety-level 4 (the highest there is) facility and what it is like to work there.

See the trailor:
(Links to Vimeo or Youtube)
Then watch the documentary! …through their blog or through microbeworld.