Translating the glycosylation code

Anabel Gonzalez–Gil always viewed science as bland memorization until she began a high school chemistry class.

“I had a professor that was very creative and we had a lot of experiments that were hands on,” she said. “That really caught my attention.”

Anabel Gonzalez–Gil

Channeling that passion, Gonzalez–Gil studied chemistry at Florida International University. As an undergraduate, she spent a summer at the University of Colorado working with calcium-sensing probes.

“That was the first time I did molecular biology and that kind of shifted my career,” she said, explaining she was captivated by being able to modulate protein expression and function.

Following a postbaccalaureate program at the National Institute on Aging, she began graduate school at Johns Hopkins University and was introduced to glycosylation, a type of post-translational modification where combinations of sugars (glycans) are added to proteins or lipids.

Most cell-surface and secreted proteins in the human body are glycosylated. The structure and density of glycans on these proteins regulate receptor binding and downstream cell signaling. Gonzalez–Gil’s doctoral work focused on the immune system, studying the receptor Siglec-8 and its glycosylated ligands in the airway.

Now as a postdoctoral fellow at Johns Hopkins, Gonzalez–Gil investigates the role of glycosylation in the brain. In the future, she plans to open her own lab.

As Gonzalez–Gil reflected on her path, she emphasized the importance of teamwork in pushing science forward. “The best of my career has not been me doing things on my own,” she said. “I would like to highlight how important and how satisfying it is to be able to collaborate.”