James C. (Jim) Paulson, PhD

Professor / The Scripps Research Institute

The Scripps Research Institute 10550 North Torrey Pines Road, MB-202 La Jolla, CA 92037

James C. Paulson is a biochemist and biologist who joined the full-time faculty of The Scripps Research Institute in 1999.


Professor Paulson’s research program focuses on the field of glycomics, and his work, for which he received the Melville L. Wolfram Award, Karl Meyer Award, Bijvoet Medal, Barnett Lecture and United States EPA Green Chemistry Challenge Award, has had a considerable impact on the treatment of cancer, influenza and bacterial infections.

Training and Education

  • 1974
    PhD, Biochemistry, University of Illinois at Urbana–Champaign
  • 1971
    MS, Biochemistry, University of Illinois at Urbana-Champaign
  • 1970
    AB, Chemistry/Biology, MacMurray College, Jacksonville, IL

Research Interests

The Paulson group investigates the roles of glycan binding proteins that mediate cellular processes central to immune regulation and human disease. The laboratory works at the interface of biology and chemistry to understand how the interaction of glycan binding proteins with their ligands mediates diverse biology in immune cell functions and virus interacting with their host cells.

Current research interests include elucidating and exploiting the roles of inhibitory Siglec receptors in immune cell responses, understanding adaptation of avian influenza viruses to human cell receptors, and investigating the glycosylation of the HIV Envelope protein in the context of recognition by broadly neutralizing antibodies.

Because glycans impact the binding of many bNAbs, understanding the details of the HIV envelope glycoprotein (Env) is critical to ensure that vaccine candidates match the glycosylation of Env on the intact virus. For the CHAVI-ID project, the Paulson lab helped characterize the recognition of glycans by a number of bNAbs using glycan microarrays.

More recently, the group has developed a method for assessing the extent of glycosylation and type of glycans at each glycosite on the HIV Env. It is currently being used to compare the glycosylation Env purified from virus with soluble SOSIP trimers and membrane bound trimers from the same strains. This information can be used to better correlate the glycosylation status of the protein with antigenicity and specificity of bNAbs – information that can inform future vaccine design.