Pamela J. Bjorkman (born 1956) is an American biochemist and molecular biologist. She is the Max Delbrück Professor of Biology and Biological Engineering at the California Institute of Technology (Caltech) and a Howard Hughes Medical Institute Investigator. Bjorkman is renowned for her pioneering work in structural biology, particularly for determining the first crystal structure of a major histocompatibility complex (MHC) class I molecule, which revolutionized the understanding of immune recognition. Her research continues to focus on the structures and functions of proteins involved in the immune system, including those relevant to viral infections like HIV, influenza, and SARS-CoV-2.
Early life and Education
Pamela Bjorkman earned her Bachelor of Arts degree in Chemistry from the University of Oregon in 1978. She then pursued her doctoral studies at Harvard University, working in the laboratory of Don C. Wiley, a prominent crystallographer. She received her Ph.D. in Biochemistry and Molecular Biology in 1984. Her postdoctoral research also took place in Wiley's lab, where she conducted the groundbreaking work on the MHC class I structure.
Career and Research
Bjorkman's most significant achievement early in her career was the elucidation of the three-dimensional crystal structure of a human MHC class I molecule (HLA-A2) complexed with beta-2 microglobulin. Published in 1987, this landmark discovery provided the first detailed atomic view of how MHC molecules bind and present antigenic peptides to T cells, a fundamental process in cellular immunity. This work was critical for understanding the molecular basis of self-non-self discrimination by the immune system.
Following her postdoctoral work, Bjorkman joined the faculty at Caltech in 1989 as an Assistant Professor, becoming a full Professor in 1995. Her research laboratory at Caltech has since expanded to investigate a wide range of immune-related proteins, employing X-ray crystallography and cryo-electron microscopy (cryo-EM) to determine their structures and infer their functions.
Key areas of her research include:
- MHC Molecules: Continuing studies on MHC class I and class II molecules, their interactions with T cell receptors, and their roles in autoimmune diseases and cancer.
- Viral Immune Evasion: Investigating how viruses, such as HIV, influenza, and cytomegalovirus, evade immune detection by manipulating MHC molecules and other host immune pathways. Her lab has characterized viral proteins involved in these evasion strategies.
- Fc Receptors: Extensive work on Fc receptors, which bind to the Fc region of antibodies. These receptors play crucial roles in antibody-mediated immunity, including maternal antibody transfer and the clearance of pathogens. Her lab has explored the structures and functions of neonatal Fc receptor (FcRn) and other Fc receptors, with implications for therapeutic antibody design.
- HIV and AIDS: Research into the structure of HIV envelope glycoproteins and strategies for developing effective vaccines and therapies against HIV.
- Influenza and SARS-CoV-2: Structural studies of proteins from influenza virus and SARS-CoV-2 to understand viral entry mechanisms and inform vaccine development.
Awards and Honors
Pamela Bjorkman's distinguished contributions to science have been recognized with numerous awards and honors:
- 1993: Presidential Young Investigator Award
- 1994: NIH Director's Pioneer Award
- 1994: Paul Ehrlich and Ludwig Darmstaedter Prize (shared with Don C. Wiley)
- 1997: Election to the American Academy of Arts and Sciences
- 2001: Election to the National Academy of Sciences
- 2002: Max Delbrück Prize for significant contributions to molecular genetics or biology
- 2006: L'Oréal-UNESCO Awards for Women in Science
- 2013: BBVA Foundation Frontiers of Knowledge Award in Biomedicine (shared with Jack L. Strominger and Don C. Wiley)
- 2021: Gairdner International Award for outstanding biomedical research.
Selected Publications
Bjorkman's work has been published in leading scientific journals including Nature, Science, Cell, and Immunity. A few highly cited publications include:
- Bjorkman, P. J., Saper, M. A., Samraoui, B., Bennett, W. S., Strominger, J. L., & Wiley, D. C. (1987). Structure of the human class I histocompatibility antigen, HLA-A2. Nature, 329(6139), 506-512.
- Bjorkman, P. J., Saper, M. A., Samraoui, B., Bennett, W. S., Strominger, J. L., & Wiley, D. C. (1987). The foreign antigen binding site of a human class I histocompatibility antigen. Nature, 329(6139), 512-518.
- Burmeister, W. P., Gastinel, L. N., Simister, M. V., Blum, M. L., & Bjorkman, P. J. (1994). Crystal structure of the basal domain of the neonatal Fc receptor at 2.2 Å resolution. Nature, 372(6504), 336-343.
- Kwong, P. D., Wyatt, R., Robinson, J., Sweet, R. W., Sodroski, J., & Bjorkman, P. J. (1998). Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature, 393(6686), 648-659.
- Stewart, C. R., et al. (2018). Structures of HIV-1 Env trimers with open and closed conformations reveal conformational changes involved in receptor engagement. Nature Communications, 9(1), 2275.