CSHL's COVID/SARS CoV2 Rapid Research Meeting Reports V

Brianna Bibel, CSHL School of Biological Sciences

The COVID/SARS CoV2 Rapid Research Reports is a series of meetings organized by Cold Spring Harbor Laboratory (CSHL) that brings together scientists from around the world to discuss the very latest research on the novel coronavirus SARS-CoV-2 and the disease it causes, COVID-19. The series began in June 2020 and continues with the sixth installment this July.

Brianna “Bri” Bibel is a fifth-year graduate student in the CSHL School of Biological Sciences studying biochemistry and structural biology in Leemor Joshua-Tor’s lab. Bri is the scientist behind the popular blog, The Bumbling Biochemist and Instagram account @thebumblingbiochemist. Her style of explaining basic biochemical experiments is approachable, and appreciated by science teachers and young students alike.

After a well-deserved break for the fourth CSHL COVID meeting which was held in Suzhou time, Bri returns to guest write for us, reflecting on the fifth installment of the meeting series:

• A short primer on viral mutation

• The B.1.1.7 variant

• The D614G variant

• Immune response and disease severity

• Antiviral therapeutics

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It’s been over a year since SARS-CoV-2, the coronavirus that causes the disease COVID-19, was discovered, and scientists are still learning new things about it daily as labs across the world dedicate themselves to unlocking the virus’ mysteries. Whether it’s determining if so-called “Variants Of Concern” are truly concerning (and if so, why), teasing apart why some people get much sicker than others, or discovering potential therapeutics to stop the disease in its tracks, there’s much to be learned. But of course, knowledge is only useful if it’s shared, and science thrives best when it isn’t siloed. CSHL’s Rapid Research Reports meetings continue to provide an opportunity for coronavirus researchers from around the world to come together, present their findings, get feedback and ideas, and maybe even strike up new collaborations.

Neil Ferguson, Imperial College London

The latest Rapid Research Reports meeting, the fifth in the series, was held virtually in January. It started with the topic that was on all our minds and in the headlines – the new coronavirus “Variants Of Concern” or VOCs. Imperial College London’s Neil Ferguson got us up to speed on what was known at the time about the B.1.1.7 variant first identified in Britain. Most of us had heard about B.1.1.7 only recently but, according to Ferguson, genomic surveillance data indicates that it actually emerged last August or September, likely in the UK, before gaining wider ground during the winter months. Unlike in the United States, where genomic surveillance has been lacking, the UK’s surveillance infrastructure was well-situated to detect when B.1.1.7 started to gain dominance. One of the reasons scientists were concerned was that it did so very quickly: By the time of the meeting, the variant was already over 50% frequency in the UK.

A short primer on viral mutation

Viruses mutate all the time because each time they replicate their genetic information (genome), there is a chance for typos. We call these typos mutations, and when you get a mutation you get a viral variant. This might sound scary, but most of the time these variants are inconsequential (or they make the virus less fit, so it can’t survive). Thus a variant, in and of itself, isn’t scary.

Sometimes however, a virus acquires a mutation that makes it more fit (e.g., allows it to spread more easily), and epidemiologists are always on the lookout for evidence of that happening. Often this evidence initially comes from genomic surveillance – scientists sequencing the RNA of random viral samples discover that a growing proportion of the samples they test are of a certain variant. When this happens, they might give that variant the “VOC” label.

Many of these VOC’s turn out to be coincidences, often the result of genetic founder effects whereby a viral variant is able to spread more widely because it “gets there first” and/or has more opportunities to spread, such as if a person sick with it attends a crowded event. In those cases, the mutations in the variant aren’t causative of the variant’s wider spread, they’re just “passenger mutations.” But the reason VOCs are concerning is because there really can be something to be concerned about – some mutations really do matter.

“...a variant, in and of itself, isn’t scary. Sometimes however, a virus acquires a mutation that makes it more fit...and epidemiologists are always on the lookout for evidence of that happening.”

The B.1.1.7 variant

At the time of the meeting, scientists were still trying to figure out whether the B.1.1.7 mutations mattered. We call B.1.1.7 a variant but it actually contains numerous variations compared to the original reference genome (the sequence of the initial sample from Wuhan). These variations include, most concerningly, mutations in the Spike protein. Often abbreviated as simply “S,” the Spike protein juts out from the viral membrane and helps the virus latch onto our cells by binding to cellular ACE2 receptors. Certain antibodies made by the immune system in response to SARS-CoV-2 infection or vaccination can bind to S in such a way as to block that docking and thus stop the virus from infecting cells. Therefore, scientists are always worried that the S protein might evolve in a way that prevents these neutralizing antibodies from binding, allowing the virus to escape the immune system. Thankfully, Neil Ferguson told us there was no evidence of such immune escape with B.1.1.7, so antibodies invoked by vaccines or natural immunity from prior infection should still be able to stave it off.

Furthermore, Ferguson told us that one S mutation in B.1.1.7 was actually fortuitous for epidemiologists because it made the variant easily spottable in the lab without requiring full-on genetic sequencing. This is because the mutation involves a deletion in part of the S gene that’s looked for by one of the diagnostic tests commonly used in the UK. The test, a PCR test, works by using short DNA probes called primers to look for several regions of viral genetic information. Because the S mutation contains a deletion in one of the primers’ binding sites, that primer would give a negative result, but the test’s other primers would give positive results so the person would still be determined positive for the virus. Using data from genomic surveillance and from the frequency of “S dropout” in the PCR results, Ferguson estimated that B.1.1.7 was about 40-70% more transmissible than the reference strain.  

The D614G variant

Another S mutation that scientists have been watching for much longer is a genetic typo leading to an amino acid change, D614G. The “D614G” nomenclature means that the RNA mutation causes the 614th amino acid (protein letter) of the S protein to be swapped from an aspartate (D) to a glycine (G). Aspartate is a big and negatively-charged amino acid whereas glycine (G) is tiny and neutral, so scientists have long suspected that this swap could affect how the protein functions and/or is processed. At the meeting, we saw evidence that this is indeed the case.

The CDC’s Bin Zhou told us that this amino acid change enhances the virus’ ability to replicate and spread, which likely contributed to D614G becoming the dominant version of S currently circulating globally. First, he showed results from experiments using purified proteins which demonstrated that D614G has enhanced binding to ACE2 compared to the original reference version. I had seen similar studies done before, but the next things he showed us I had never seen, and they were really cool! Zhou did competition experiments in which he pitted the D614G-containing virus against the original under different conditions and saw which won out. He started with cell culture experiments – when he treated cells with equal amounts of D614G and original virus and then observed which became dominant in the cell culture, D614G won every time. Even if he started with 9 times more of the original, the D614G variant was able to gain ground. But does that correspond to real, in vivo, effects? Zhou showed results from competition experiments in hamster and ferret models of SARS-CoV-2 infection as evidence that yes, it does: In the animal models, D614G outcompeted the original and was able to spread better from animal to animal.

Sophie Gobeil, Duke University School of Medicine

But why? Could hints be in the spike’s structure? Sophie Gobeil, a postdoctoral researcher in Priyamvada Acharya’s lab at Duke University School of Medicine, thinks so. She presented a poster of work she and colleagues had done characterizing the effects of D614G at the structural level. Using cryo-electron microscopy (cryo-EM), they got high resolution looks at the original and D614G versions of the S protein. One thing to know about S is that it’s a homotrimer, meaning it’s made up of three identical subunits working together. Each of these subunits contains a receptor binding domain (RBD) which, if in the “up” conformation, can bind to cellular ACE2 receptors, allowing the virus to dock onto our cells. Gobeil found that, compared to the original S, the D614G S protein was more likely to have an RBD in the up conformation, and thus was more “ready” to bind ACE2. The amino acid change is far from the RBD itself, which Gobeil says indicates local disturbances to accommodate the glycine led to ripple effects elsewhere in the protein – a phenomenon biochemists refer to as allostery.

Although the amino acid swap-out is far from the RBD, it’s near the furin cleavage site. Furin is a sequence-specific protease (protein-cutter), and the furin cleavage site is a location on the protein that contains the sequence furin likes to cleave. Gobeil presented evidence that the D614G change enhanced cleavage by furin. Why might that matter? Antoni Wrobel, a postdoctoral researcher in Steven Gamblin’s Lab at the UK’s Francis Crick Institute, has some ideas – and data! Wrobel showed us how this cleavage loosens up S in a way which primes it for fusing with the cell’s membrane and dumping the virus’ contents into the cell. 

If the D614G variant is more easily cleaved by furin, as Gobeil showed, then it would then be primed more often, as Wrobel showed, and this could help explain some of the increased transmissibility Zhou saw in his challenge studies. It was great to see different avenues of research from researchers around the world coming together to help piece together this scientific puzzle!

“...different avenues of research from researchers around the world [came] together to help piece together this scientific puzzle!”

Immune response and disease severity

Speaking of puzzles, one of the most puzzling things about SARS-CoV-2 is that it affects people so differently, with some developing severe pneumonia while others don’t even know they’re infected. To investigate why this is the case, scientists have dissected the immune system response in patients spanning the entire spectrum of disease severities, and at the meeting we got to hear from some of the immunologists leading this charge.

“Patients with COVID have high levels of...autoantibodies against many cellular proteins, including the immune system’s own proteins.”

James Heath, a scientist at the Institute for Systems Biology, told us about a deep, longitudinal analysis he was doing on the blood of around 200 COVID patients with a full range of disease severities. His group collected blood samples from patients at time of diagnosis, 1 month later, and 2-3 months later, then performed as many experiments as possible to try to determine everything that was in the blood: Proteomics to study the proteins present, metabolomics to look at small chemical products of metabolism, even single-cell secretome tests to see what signaling molecules cells released. Heath fed all that data into his computer and asked it to look for trends. When he did this, he found distinct signatures of mild vs. moderate disease, and also saw evidence of a lingering immune response in patients with moderate to severe COVID months after the original infection.

And that’s not the only evidence of immune system dysregulation seen in COVID patients. One thing that became apparent early on in the pandemic was that many of the sickest people were suffering not from the viral attack itself per se, but from their own immune systems. We usually think about antibodies as being “good,” such as anti-S antibodies binding to the Spike protein. But not all antibodies are good – they’re only good if they target things that are “bad.” Antibodies against one’s own proteins are called autoantibodies and they can cause the immune system to attack the body, destroying cells and tissues. Evidence from a number of labs shows that patients with COVID have high levels of such autoantibodies against many cellular proteins, including the immune system’s own proteins.  

Aaron Ring, Yale School of Medicine

Because there are so many different proteins these antibodies could be binding to, it has been hard to measure and characterize them, but Yale’s Aaron Ring told us about a system he developed to do just that. Named Rapid Extracellular Antigen Profiling (REAP), the basic idea is to get yeast cells to make human proteins and display them from their surface. More specifically, each yeast cell displays a different human protein and contains a corresponding DNA barcode, which Ring can sequence to infer what protein was displayed. He then mixes a patient sample with the yeast cells. If that sample contains antibodies targeting human proteins, those autoantibodies will bind to the yeast cells displaying those proteins. He can then isolate the antibodies and any bound yeast, and use DNA sequencing to see what human proteins the antibodies were stuck to.

Using this system, Ring confirmed and expanded the findings of other researchers showing that patient samples contained high levels of autoantibodies targeting proteins on the surface of immune cells. He presented evidence that these autoantibodies lead to the depletion of specific populations of immune cells, contributing to immune system dysfunction. He also found autoantibodies against proteins that are prevalent in a variety of tissues known to be affected by COVID, including tissues of the vascular system, heart, lungs, and central nervous system. The autoantibody signatures were different for different patients, and he’s following up on these findings to determine whether levels of these tissue-specific autoantibodies are associated with specific symptoms. He’s also tracking autoantibodies from samples taken over time to figure out whether they may be implicated in post-COVID syndrome (aka long COVID). Because the technology is so new, he doesn’t yet know how much of what he sees is specific to COVID as opposed to being a general viral response, but he’s eager to test samples from patients recovering from other viruses in order to find out!

“[Teams of scientists] are hard at working tyring to discover new antiviral therapeutics, especially ones that can be taken on an outpatient basis.”

Antiviral therapeutics

With all the talk of vaccination in the news, it’s easy to forget that there’s a whole other pharmacological aspect to confronting the pandemic which we will still need as long as the virus is around – namely, treatment. But teams of scientists around the world aren’t forgetting. Instead they’re hard at work trying to discover new antiviral therapeutics, especially ones that can be taken on an outpatient basis. At the meeting, we got to hear some of the latest prospects.

John Chodera, Memorial Sloan Kettering Cancer Center

One of my favorite talks was from John Chodera, a computational chemist at Memorial Sloan Kettering Cancer Center. Chodera told us about the “COVID Moonshot” project, which uses crowdsourcing to develop an inhibitor of the SARS-CoV-2 main protease (MPro). SARS-CoV-2 has many proteins, but it makes them as a long chain of connected proteins called a polyprotein. In between different proteins in the chain are protease cleavage sites, and the virus gets our cells to make the specific protease that recognizes them; block that protease and the virus can’t separate its proteins and thus can’t replicate. The goal of the COVID Moonshot project is to develop molecules that can to do just that.

I’d actually been following this project for a while, so it was great to hear a talk from one of the leaders. The basic story is that scientists at the Diamond Light Source in the UK soaked crystals of MPro with a compound fragment library (basically little drug-parts). Some of those fragments bound to MPro and the scientists used x-ray crystallography to solve crystal structures showing, at the atomic level, where those fragments bound in the protein. They then uploaded their data and asked volunteers to try to connect and/or modify the fragments to design drugs that could bind better and hopefully inhibit MPro. The team used an AI tool called PostEra to predict which designs would be easiest to make, then selected the most promising designs, synthesized the molecules, and tested them. In their first round, over 350 designers submitted a total of more than 7,000 molecules and the team synthesized and tested over 800 of them, finding promising leads that they then followed up with optimization.

Amanda Hargrove, Duke University

We also heard talks on other potential treatments that I hadn’t heard of before. For example, Duke chemist Amanda Hargrove told us how her lab is developing small molecules that target the coronavirus’ RNA. We often think about RNA as long strands, but those strands fold up into functional 3D shapes. SARS-CoV-2 has multiple stem-loop folds that are crucial for viral replication, and Hargrove is working to create molecules that specifically bind those structures and inhibit replication. The work she presented was based off of knowledge she’d gained while doing similar experiments to target HIV RNAs; in addition to potentially treating COVID, the knowledge she gains from her current work can likely be used to help treat other diseases with some tweaks of the molecules’ chemistry. RNA-binding drugs are definitely an exciting field to keep an eye on!

Speaking of keeping an eye on things, I can’t wait to see what’s in store at the next Rapid Reports meeting!

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This post is part of a series, and here is a summary of the first, second, and third COVID meetings.

The next installment of the CSHL COVID/SARS CoV2 Rapid Research Reports meeting series will take place on July 7-8, 2021.

Visitor of the Week: Julia Nepper

Meet Julia Nepper of the Wisconsin Institute for Discovery at the University of Wisconsin-Madison! Julia is a postdoctoral trainee in Jo Handelsman’s lab and is with us this week at The Biology of Genomes meeting. This is Julia’s first meeting at CSHL and she presented a poster titled “Genetic regulation of soil microbe biofilm formation in response to sublethal antibiotic treatment”.

Tell us about your research.
My research centers around understanding how the chemicals that soil bacteria produce allow them to communicate with each other. Specifically, I study a system of bacteria that models the rhizosphere, the area of soil on and immediately surrounding plant roots.

How did you decide to focus on this area/project?
It’s been an interest of the lab for a long time, and there were preliminary results suggesting that some signal was causing a biofilm phenotype in one of the bacteria from our model system. Because I had previous experience with biofilm research, I decided to investigate further.

What and/or who is the inspiration behind your scientific journey?
I’ve been interested in science ever since I could remember, and that passion was nurtured and supported by my parents throughout my childhood education. My undergraduate research experience convinced me to pursue a PhD. When I finish my work with Prof. Handelsman, I’m hoping to pursue a career in communicating science to lay audiences.

What impact do you hope to make through your work?
I’m hoping that my work will pave the way for a better understanding of bacterial biofilms and communication. Our goal is to establish a model system that can be used by researchers across the globe to interrogate rhizosphere bacterial dynamics in a controlled and methodical manner.

Where do you see yourself in five years?
I would love to be the host of a podcast/video series about science in general, but especially biology.

What do you love most about being a researcher?
I love talking to other people about research, and learning not just about the science, but also about the human stories that are behind the work.

What drew you to attend this meeting?
It was brought to my attention by my training grant program director. It seemed like a great opportunity to learn more about what’s state-of-the-art in terms of genomic and transcriptomic research. I am still fairly new to ‘omics, so I appreciate any chance to improve my understanding of the area.

What is your key takeaway from the Meeting; and how do you plan to apply it to your work?
I found an interesting poster that discussed different methods for RNA sequencing with low input concentrations. Although the work was done in the context of immune cells, I think it could easily be applicable to my work with bacterial biofilms.

What feedback or advice would you share with someone considering to participate in this meeting?
Although it can be tempting to stick to the subject areas related to what you study, sometimes it’s fun to go to a “random” talk or poster and learn something totally new! And you never know when those insights can actually be super useful for thinking about your work in a different way.

What’s the most memorable thing that happened during the Meeting?
I virtually “ran into” an old colleague of mine and we had a great discussion catching up on what we’ve been working on the past few years.

Thank you to Julia for being this week's featured visitor. To meet other featured researchers - and discover the wide range of science that takes part in a CSHL meeting or course - go here.

Image provided by Julia Nepper.

Visitor of the Week: Chandler McElrath

Meet Chandler McElrath of the Medical College of Wisconsin! A member of Dr. Adriano Marchese’s lab within the Department of Biochemistry, Chandler joins us this week for the Ubiquitin, Autophagy & Disease virtual meeting. This is the first CSHL meeting for the second year graduate student and also her first time interacting with the ubiquitin community as a whole.

Tell us about your research.
I’m interested in how ubiquitin regulates GPCR signaling and trafficking. I study this in the context of the chemokine receptor CXCR4 and cancer metastasis.

How did you decide to focus on this area/project?
I had two undergraduate research experiences, studying the ubiquitin-proteasome system and GPCR signaling, respectively. I was thrilled to be able to find a dissertation lab where I could study both of these topics.

What and/or who is the inspiration behind your scientific journey?
I would not be where I am today without Dr. Jamie Scaglione. In addition to serving as my undergraduate academic advisor, she presented me with my first research opportunity at Carroll University which sparked my love for research. In 2017, this project extended into a summer experience in the laboratory of Dr. Matt Scaglione at the Medical College of Wisconsin (now Duke University) where I was introduced to the ubiquitin proteasome system. Fantastic mentorship propelled me into my PhD studies at MCW. As a professor someday, I hope to be able to do the same for my students.

Where do you see yourself in five years?
I will have graduated from MCW with my PhD and pursuing my career as a biochemistry professor focusing on undergraduate instruction.

What do you love most about being a researcher?
I love being able to ask and answer questions that no one else has before and contribute to the world’s understanding of how our cells operate.

What drew you to attend this meeting?
Ever since one of my undergraduate research experiences, I have been particularly interested in the ubiquitin proteasome system. I picked my dissertation project based off this interest, and I am excited to attend a conference with a group of people all passionate about similar subjects!

What is your key takeaway from the Meeting; and how do you plan to apply it to your work?
I learned quite a bit about ubiquitin binding domains to detect different types of ubiquitin chains, and this will prove useful for developing protocols in our lab to learn more about how ubiquitin is involved in GPCR regulation.

What feedback or advice would you share with someone considering participating in this meeting?
Take the time to integrate information that you learn at poster sessions and at seminars!

What’s the most memorable thing that happened during the Meeting?
This was my first time interacting with other professionals in the ubiquitin community, and everyone was so welcoming and willing to answer my questions. As a young graduate student, it was neat to directly communicate with people whose publications I cite frequently! I look forward to meeting everyone in person at a future meeting.

Thank you to Chandler for being this week's featured visitor. To meet other featured researchers - and discover the wide range of science that takes part in a CSHL meeting or course - go here.

Image provided by Chandler McElrath.

Visitor of the Week: Kathleen Abadie

Meet Kathleen Abadie of the University of Washington! She is fourth year graduate student in the bioengineering department and a member of Hao Yuan Kueh’s lab. Kathleen joined us at last week’s Systems Immunology meeting — her second Systems Immunology meeting — where she presented her first talk as a graduate student titled “Early CD8 T cell fate programming revealed by time-resolved RNA sequencing and time-lapse imaging in single cells.” Here’s what she shared about that experience:

This was my first time giving a talk at a conference as a grad student. It was a great experience, and I’ve been so grateful to people who have reached out with questions and ideas. It’s a nice reminder of how supportive and collaborative the scientific community is.

Tell us about your research.
I research T cell fate decisions – that is, how does a single naïve T cell that encounters a foreign pathogen give rise to multiple populations of functionally distinct progeny in ratios that are tuned to the nature of the threat? This question is relevant for better understanding and subsequently engineering T cells for therapy and also for understanding broader gene regulation principles in differentiation.   

How did you decide to focus on this area/project?
I worked at a pharma company before grad school (Genentech), where I found inspiration both in scientific curiosity and the potential to bring new, better therapies to patients. When I decided to go to grad school, I wanted to work in an area that was exciting both for the pure biology and for the therapeutic potential. T cells are just that! The immune system, and T cells in particular, have so many amazing properties to explore, and the potential of engineered T cell immunotherapies to revolutionize treatment for cancer and other diseases is really exciting to me.

What and/or who is the inspiration behind your scientific journey?
Thanks for asking this. It’s always nice to reflect on why we are where we are. When I look back on my scientific journey, what really stands out are the mentors I’ve had who have shared their own scientific excitement with me, helped me find my own, and given me real-life examples of what I see as a satisfying and successful scientific career. I can think of a handful of people who just lit up my brain when we talked, and I’m so lucky to have had those influences. One of these is my current PI, Kueh!

If Kathleen is not in the Lab, she’s usually on the bike!

What impact do you hope to make through your work?
I have a few answers to this. I hope to someday be able to provide the same inspiration to developing scientists as the people I mentioned above provided to me. I also hope to contribute new ideas to the field of immune cell fate control and immunotherapy. Lastly, I hope I can play a small role in the big and exciting task of engineering T cells to treat disease. 

What do you love most about being a researcher?
I love facing a totally unknown problem and thinking about how to creatively address it. On the flip side, this is probably also the most painful part of being a researcher for me. It’s so hard to know that what I am doing is ‘useful’ or ‘the right direction,’ which causes a lot of angst. I think in the end, dealing with this paradox will make me a better and stronger person (at least, that’s what you have to tell yourself in the low points of grad school).

What drew you to attend this meeting?
This meeting is such an exciting union of different fields – basic immunology, genomics, mathematical modeling. It’s amazing to see all the techniques and expertise come together here and listen to people share ideas across fields. I think the potential for synergistic progress here is vast, and I want to be a part of it!

What is your key takeaway from the Meeting; and how do you plan to apply it to your work?
A big takeaway for me is that there are a lot of creative ways to analyze data, particular those so high dimensional and rich as single-cell sequencing data. I should consider how these techniques could help me get more out of my data, even though it is often intimidating to get a new computational technique up and running in my hands.

What’s the most memorable thing that happened during the Meeting?
It’s a toss-up between Ron Germain playing a Joni Mitchell song in the middle of his talk and Uri Alon singing about autoimmune surveillance of hyper-secreting mutants.

Thank you to Kathleen for being this week's featured visitor. To meet other featured researchers - and discover the wide range of science that takes part in a CSHL meeting or course - go here.

Images provided by Kathleen Abadie.

Visitor of the Week: Marjan Farahbod

Meet Marjan Farahbod of Simon Fraser University (Canada). The postdoctoral fellow is a member of Dr. Maxwell Libbrecht’s lab where research focuses on gene annotation. Marjan joins us at this week’s Probabilistic Modeling in Genomics virtual meeting – her first meeting at CSHL.

Tell us about your research.  
I am working on obtaining a better understanding of gene regulatory mechanisms using epigenomics data. In particular, I am trying to understand gene regulatory mechanisms in lung function and COPD (Chronic Obstructive Pulmonary Disease).

How did you decide to focus on this area/project?
During my PhD, I worked on the inference of gene function and regulation from transcriptomic data. I am interested in gene regulatory mechanisms, data characterization and method development--this project has all these elements to various degrees. In recent years multiple epigenomics datasets have become available, making it possible to study gene regulation using this form of data. There is much work to do here and I am excited about it.

What and/or who is the inspiration behind your scientific journey?
My mentors and colleagues. Then there is the curiosity, the complexity and the never-ending thread of questions; along with the creativity and the ideas that lead to the answers!

What impact do you hope to make through your work?
I admire the collective effort of researchers to find answers and solve problems, and I see my work as a small contribution to this effort. I hope to share my skills and ideas, lead projects and inspire.

Where do you see yourself in five years?
As a relatively new postdoc, my contribution to the field has been mostly my research products in the form of publications. In the next five years, I hope to inspire and lead new research efforts.

What do you love most about being a researcher?
Perhaps being surrounded by the excitement of the unknown. The abundance of questions, and that there is always something interesting going on. Research can be intimidating too. Sometimes I find myself overwhelmed by how much I don't know at the beginning of a project, but once I start the actual research, the curiosity takes over. 

What drew you to attend this meeting?
The meeting was a great opportunity to hear from the experts in my field and learn about its recent advancements. Specifically, it was great to hear from Professor Anshul Kundaje on their work in motif syntax, this is relevant to my project and something that I will look into. 

What is your key takeaway from the Meeting; and how do you plan to apply it to your work?
At the end of her keynote talk, Professor Daphne Koller briefly talked about the key advancements in different fields through time, and where we are today in our field. Her description resonated with me and was inspiring.  We are in a unique era, where the technical advancements in high-throughput biology and machine learning allows us to ask questions that we were not able to ask 10 or even 5 years ago. To think what will be possible in the near future, and how many questions we will be able to answer is exciting. 

What feedback or advice would you share with someone considering to participate in this meeting?
Perhaps not specific to this meeting, but usually for me the keynote talks provide high-level views of the field and its challenges so I try to attend all of them, even if they are not directly related to my research. For the talks, I attend the sessions that are most relevant, and those are usually from the authors or labs that I know of or am familiar with their work. Posters are even more focused, and there is a chance to have in-depth conversations on specific approaches or datasets in the poster session.

What’s the most memorable thing that happened during the Meeting?
I think attending the meeting in its virtual form will be quite a memorable experience. I appreciate the efforts that went into the arrangement of such a setting. I particularly liked the pictures from the mission control posted on the Slack! It was also cool that everyone was just a Slack message away.

Image provided by Marjan Farahbod.

Thank you to Marjan for being this week's featured visitor. To meet other featured researchers - and discover the wide range of science that takes part in a CSHL meeting or course - go here.