Vilde Leipart is a researcher at Norwegian University of Life Sciences in Ås. She shares her AlphaFold story.
I feel strongly about the need to protect honeybees.
Honeybees are so integral to our culture and to our economy, but most importantly, to our ecosystems. The survival of many species is dependent on them as pollinators. But around the globe, honeybee populations are rapidly declining due to environmental factors and human interference.
To increase their chances of survival, we need to study the fundamentals of the bee immune system. My area of interest is vitellogenin, a protein you can find in pretty much any animal that lays eggs. It supports reproduction, but also appears to play other roles, including immunity and regulating feeding behaviour.
Vitellogenin can bind to pathogen proteins like an antibody and contributes to immunity that is passed on in egg-laying species. Fragments of bacteria, fungi and viruses, ingested by the mother – or queen – are transferred into developing eggs where they trigger immunity in the developing embryo. This ‘trans-generational immune priming’ is key to increasing the survivability of honeybees – and many other species – in a world full of infectious diseases.
"It took me two days to do something that could have taken me years."
- Vilde Leipart, life sciences researcher
Lamprey vitellogenin was modelled in the late 1990s using x-ray crystallography. Until now, though, little was known about the structure of the honeybee version, which is a hard protein to map, mainly because it is very large. So we set out to use AlphaFold to understand it.
Because vitellogenin appears to play many roles, we wanted to visualise its function-specific domains, see how they interact, and then make predictions about their different functions based on the structure revealed by AlphaFold. I learned so much from the structure that AlphaFold created – I have spent so many hours staring at it. I am still learning! We were able to see how the full length of the protein is assembled and connected and how the protein subunits interact. The key thing is how quickly I was able to do it. It took me two days to do something that could have taken me years.
This work has broader implications too. Egg-laying species include tree frogs, chickens, crocodiles, ghost sharks and turtles. They all make vitellogenin and are all vulnerable to a variety of infectious diseases. Understanding its basic functions in honeybees may reveal what it does in other animals, and through that, help protect vulnerable wild species and domestic farm animals from infectious diseases and pesticides.
I love studying honeybees and hope this research can lead to new ways of protecting this species and others. I live and work in Norway. Here, fish and fishing are really important to our culture and our economy. Fish – especially commercially farmed fish – are vulnerable to disease outbreaks and I want to expand my research to work on salmon vitellogenin and, I hope, make a difference.
This work, made possible by AlphaFold, has implications for such a wide range of species and scenarios, it’s really exciting.