Julia Van Der Marel

Julia Van Der Marel

Biography

Julia Van Der Marel is a rising junior at the University of Maryland, Baltimore County,
pursuing a degree in Chemical Engineering on the Biotechnology track. She is a member of
the NIH U-RISE Scholars Program, the UMBC Meyerhoff Scholars Program, the UMBC
Honors College, and Tau Beta Pi, where she strives to contribute to a diverse and inclusive
scientific community. Her background as a type 1 diabetic drives her to pursue a Ph.D. in
immunology, with a focus on diagnostics, treatment, and prevention. At her home institution,
she works as a researcher at the Center for Advanced Sensor Technology with Dr. Govind
Rao. Her team’s current research project is focused on cell-free protein synthesis, a nascent
alternative to cell-based biomanufacturing. Over the summer, she worked with Dr. Brandon
DeKosky and Gaurav Awasthi of the DeKosky lab to research the optimization of anti-HIV
antibody binding affinity and breadth through yeast display.

Optimization of Anti-HIV Antibody Binding Affinity and Breadth
Through Yeast Display
Julia Van Der Marel1, Gaurav Awasthi2, Francisco Figueiras3, Brandon DeKosky2,3
1Department of Chemical, Biochemical, and Environmental Engineering,
University of Maryland, Baltimore County
2Department of Chemical Engineering, Massachusetts Institute of Technology
3The Ragon Institute of Massachusetts Institute of Technology, Massachusetts General
Hospital, and Harvard

Creating a vaccine against Human Immunodeficiency Virus (HIV) remains a matter of great
public health importance, with 40.9 million people worldwide living with HIV as of 2025. The
exceptionally high mutation rate of HIV necessitates a vaccine which can cover genetically
diverse strains. The N6 antibody is one of the broadest anti-HIV antibodies identified, capable
of neutralizing 98% of HIV isolates. Its breadth is derived from its binding to the relatively
conserved CD4-binding site on the HIV envelope glycoprotein. This lab previously created
libraries of yeast cells which display antigen-binding fragments of mutated N6 on their surface.
These libraries allowed for high-throughput screening with flow cytometry to select antibody
candidates that bind to an HIV antigen already strongly-neutralized by N6. This research
project used successive rounds of sorting with sequentially lower antigen concentrations to
select antibodies with higher affinity to this antigen than the unmutated N6 antibody. Now
that the highest-affinity binders have been selected, the lab will sort against different antigens
which are resistant to or poorly neutralized by N6 to find antibodies with increased breadth
against more HIV strains. These successive rounds of sorting will be used to isolate antibody
candidates with enhanced affinity and breadth.