Biophysical Society Bulletin | February 2026

Biophysicist in Profile

Eric Sundberg Area of Research The role of glycans in antibody-mediated effector functions

Institution Emory University

At-a-Glance

Eric Sundberg ’s career evolved from teenage research in his father’s chemical engineering lab to leading work on antibody engineering at Emory University, where he now serves as professor and chair of biochemistry. His research focuses on manipulating glycans on immunoglobulin G (IgG) anti bodies to develop new therapeutics for autoimmune diseases, while finding his greatest rewards in mentoring trainees and supporting young faculty.

Eric Sundberg

Eric Sundberg ’s path to becoming a leading structural immu nologist began in his father’s chemical engineering lab at the University of New Hampshire. At the age of 16, Sundberg found himself filling a gap left by departing graduate stu dents, working on interfacial energies in multi-component latex particles. What started as a summer job evolved into a formative experience that would span multiple years and produce his first peer-reviewed publication—co-authored with just one other person. “My first peer-reviewed journal article, with just two authors (both named “Sundberg!”), was published when I was in college but describes work that I did while a high schooler,” he recalls. This early immersion in re search, facilitated by his father’s polymer engineering exper tise, provided a foundation that would eventually lead him far from latex particles and into the intricate world of antibody engineering and immune system function. His pivot to biophysics came during Sundberg’s undergradu ate years at the University of Rochester, where he balanced rigorous academics with his role as captain of the men’s soc cer team. In a graduate course on bioorganic chemistry taught by Eric Kool , Sundberg first encountered three-dimensional protein models visualized on a computer screen. “When he told me that X-ray crystallographers generate most of the protein structures that we were looking at and spinning around on the screen, I decided there and then to go to grad uate school to learn crystallography,” Sundberg explains. That decisive moment led him to pursue dual bachelor’s degrees in biochemistry and economics—finding both topics fascinat ing—before committing fully to structural biology. At Northwestern University, Sundberg became the first PhD student of Ted Jardetzky , who had recently completed postdoctoral work with the late Don Wiley at Harvard. This positioned Sundberg at the cutting edge of structural im munology, where he tackled problems involving molecular recognition, host immunity, and host-pathogen interactions while solving his first X-ray crystal structure.

His postdoctoral work with Roy Mariuzza at what is now the Institute for Bioscience and Biotechnology Research in Rock ville, Maryland, deepened this expertise. Sundberg describes moving “from one structural immunology lab to another, extending my studies on how the human immune system and human pathogens interact, solving many more crystal struc tures, and expanding my biophysical skillset.” The research that would come to define Sundberg’s career emerged from a fortunate lab placement. After launching his first independent lab at the Boston Biomedical Research Institute and subsequently moving to the University of Mary land School of Medicine and the Institute of Human Virology in Baltimore, Sundberg found his lab located next to that of Lai-Xi Wang , an expert in glycan remodeling. Wang’s work focused on the conserved glycan found on IgG antibodies—a sugar modification that controls how these an tibodies interact with Fc gamma receptors and complement proteins, thereby determining their effector functions. The collaboration that emerged from this proximity would prove transformative. Together, they determined the high-resolu tion structure of EndoS, an IgG-specific endoglycosidase, and defined how these enzymes achieve their remarkable speci ficity for IgG antibodies. “We teamed up with Lai-Xi and his group to determine the high-resolution structure of EndoS and went on to define the molecular basis by which these enzymes achieve strict IgG substrate specificity, discover a new family of IgG-specific en doglycosidases, and turned them into potential therapeutics to treat autoimmunity and other IgG-mediated pathologies,” Sundberg shares. Now professor and chair of biochemistry at Emory University School of Medicine, Sundberg’s research has evolved to focus on what he describes as “defining the molecular basis of, and engineering, antibody-mediated effector functions.” His group is pushing the boundaries of enzyme engineering, as

February 2026

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