Q&A with Michael Grunst PhD ’25
Grunst received the university's John Addison Porter Prize for his dissertation on viral Spike proteins.
June 9, 2025

Michael Grunst PhD ’25 (Microbiology) has spent the last nine years studying viruses, first at an HIV lab at the University of Wisconsin-Madison, and then as a PhD student in the Microbiology program at Yale. He arrived in New Haven shortly before the COVID-19 pandemic lockdown, an opportune time for someone interested in virology.
His dissertation focused on viral Spike proteins, which allow viruses to grab onto and enter host cells through driving fusion of the virus and host cell membranes. The research has implications for future vaccine development and cures to persistent viral infections.
In May, his work was honored at the Graduate School’s Convocation Ceremony with the John Addison Porter Prize, considered to be one of the university’s most prestigious awards.
We sat down with Grunst to learn more about his research process, his journey to Yale, and what’s next in his career.
How did you become interested in studying coronaviruses?
I started working in an HIV lab at the University of Wisconsin–Madison in 2016, studying how antibodies protect us from infection. When I came to Yale, my advisor’s lab had pivoted to coronavirus research during the pandemic. That’s when I got involved in studying how antibodies interact with viral Spike proteins.
What role do Spike proteins play in coronavirus infection?
Coronaviruses are decorated with these proteins on the outside, called Spike proteins, which allow the virus to grab onto to host cells via host cell receptors. They undergo changes that help fuse the virus and the host membranes together so the virus can enter the cell. Most antibodies that protect us from infection work by binding to these proteins and preventing the virus from attaching to cells. The Spike protein is the basis for the coronavirus vaccines we have currently. And that's how most antibodies seem to work, with a lot of different nuances in there.
How does this inform vaccine design?
Some antibodies that protect us against infection work in different ways. They don't necessarily prevent the virus from binding to its host receptor. The reason we care about those antibodies is because some of them bind to highly conserved epitopes, which are regions where the sequence of the protein is similar. From new variant to new variant, these areas will stay the same and these antibodies will still bind consistently.
This is important because when the coronavirus Spike protein mutates, our vaccines become less effective. When we're thinking about developing pan coronavirus vaccines, a lot of interest is on these highly conserved epitopes. They seem to be so important for the function of the protein that the virus cannot easily mutate and escape, because if they were to do that, then it might lose function.
Tell us about your research study.
There’s been broad interest in these antibodies that bind to this region for a long time, but other groups never got at the question of how exactly they work. Our study was trying to get at that mechanism. We used cryo-electron microscopy to image these tiny events in high molecular detail. We could actually see how these antibodies are binding to the Spike protein as it was changing form and shape during the fusion process.
We collaborated with fantastic molecular dynamics teams at Northeastern and Rice University who performed computer simulations. We had reached out to them and found that our data corresponded very well. So we developed these models together.
What are the implications for new vaccines?
Understanding how these antibodies work could help us design new vaccines that target conserved regions of the Spike protein. That would make them more effective against future variants or even other coronaviruses.
How did you first get into virology?
It was a bit of a fluke. I was working with the Forest Service in California, doing fire ecology. At the end of the summer, I needed a new job and found one in a virology lab at the University of Wisconsin–Madison. I had studied biochemistry as an undergrad, so it seemed like a good idea.
What brought you to Yale?
I knew of researchers here doing great work in HIV, like Priti Kumar and Walther Mothes. I applied to work with labs doing interesting research based on publications I had read.
What was your lab experience like?
Walther gave us a lot of freedom to think about different questions and different ways to answer them. I learned everything I know about cryo-EM from a senior lab member, Wenwei Li. It’s a lot of computer work and some coding. He was very patient in teaching me from the ground up. Professor Pradeep Uchil was also a key mentor in the lab for other non cryoEM-related skills. The mentorship in the lab was great.
Were you involved in the broader Yale community?
Yes, I was part of the Gruber Science Fellows community, and I earned a teaching certificate from the Yale Poorvu Center. I also completed the Yale Science Communication program, through which I gave presentations at public libraries. The ability to communicate with a lay audience is a really important skill.
What’s something you wish more people knew about your field?
That scientists are genuinely curious and passionate about understanding how things work. We’re not driven by money—we just love the science.
What are your post-Yale plans?
I’m applying for postdoctoral fellowships now. I’m looking at opportunities both in the U.S. and abroad.
Any final thoughts?
I’m grateful for everyone who supported my work and for the people that recognized it and thought it was important.