Office 321 RAL
(enter through 323)
Mail to: Roger Adams Laboratory Bldg,
600 S. Mathews Avenue, MC-712 B-4
Urbana, IL 61853
Assistant Professor of Biochemistry
Host-Pathogen Interactions, Molecular Immunology, Protein Dynamics, Protein Structure, Virology
Disease Research Interests
B.S. 2003 University of Wisconsin, Madison
Ph.D. 2010 University of Utah
Postdoc. 2011-2018 California Institute of Technology
Announcement: The Stadtmueller Lab formed in Fall 2018 and is growing! The lab is currently accepting graduate rotation students and applications for postdoctoral fellows. Undergraduate positions will be available beginning January 2020. If you are interested in joining the lab please email firstname.lastname@example.org.
Specific Research Areas:
Antibody structure, antibody engineering, mucosal immunology, retroviral envelopes, electron paramagnetic resonance, electron microscopy, X-ray crystallography
Host-microbe coevolution has produced intricate interspecies relationships in which countless host and microbial proteins interact, ultimately influencing the fitness of both species. Yet, the molecular mechanisms that define many host-microbe interactions remain unexplored, limiting our ability to understand and influence health and disease. To address this challenge, the Stadmueller Lab studies proteins and protein complexes found in the immune system, bacteria and retroviruses using an approach that combines structural biology and biophysics, (e.g. X-ray crystallography, electron microscopy and electron paramagnetic resonance spectroscopy) with protein engineering and animal models of disease.
The lab focuses on two specific biological topics: (1) We investigate the unknown structures and mechanisms of the predominant mucosal antibody, secretory IgA (SIgA), in order to determine how its poorly understood, polymeric architecture can support both pathogen clearance and commensal microbe homeostasis and how we can engineer antibody-based therapeutics to modulate these two functions. (2) We investigate endogenous retroviral envelope (env) proteins, fusogenic proviral proteins expressed from ancient retroviral DNA elements that have integrated into host genomes over millions of years, in order to determine how retroviral env structures and mechanisms have been co-opted through host evolution to support endogenous functions (e.g. embryo implantation) and how they contribute to disease states such as cancer and HIV infection. The broad, long-term goal of these two projects is to understand how protein structure and function has shaped the relationships between the vertebrate immune system, bacteria and viruses and using that information, to develop protein-based therapeutics that can modulate host-microbe interactions.
Stadtmueller B.M., Bridges M.D., Dam K-M., Lerch M.T., Huey-Tubman K.E., Hubbell W.L., Bjorkman P.J. (2018) DEER Spectroscopy Measurements Reveal Multiple Conformations of HIV-1 SOSIP Envelopes that Show Similarities with Envelopes on Native Virions. Immunity. 2018 Jul 26. [Epub ahead of print] https://www.ncbi.nlm.nih.gov/pubmed/30076100
Stadtmueller, B.M., Yang, Z., Huey-Tubman, K.E., Roberts-Mataric, H., Hubbell, W.L., and Bjorkman, P.J. (2016). Biophysical and biochemical characterization of avian secretory component provides structural insights into the evolution of the polymeric Ig receptor. J Immunol. 197(4): 1408-1414. http://www.ncbi.nlm.nih.gov/pubmed/27412418 Featured “In this Issue:” http://www.jimmunol.org/content/197/4/1007
Stadtmueller, B.M., Huey-Tubman, K.E., Lopez, C.J., Yang, Z., Hubbell, W.L., and Bjorkman, P.J. (2016). The structure and dynamics of secretory component and its interactions with polymeric immunoglobulins. eLife 5. https://www.ncbi.nlm.nih.gov/pubmed/26943617 Featured in Caltech News: https://www.caltech.edu/news/multitasking-protein-keeps-immune-system-healthy-51946
Stadtmueller, B.M.*, Kish-Trier E.*, Ferrell K., Robinson H., Myszka D.G., Formosa, T. Hill, C.P. (2012) Crystal structure of the Pba1/2-proteasome complex and implications for HbYX-dependent proteasome interactions. J Biol Chem 287(44):37371-82. https://www.ncbi.nlm.nih.gov/pubmed/22930756
Stadtmueller, B.M. and Hill, C.P. (2011) “Proteasome Activators.” Mol Cell 41(1): 8-19. https://www.ncbi.nlm.nih.gov/pubmed/21211719
Stadtmueller, B. M., Ferrell K., Whitby F.G., Heroux A., Robinson H., Myszka D.G., Hill C.P. (2010) Structural models for interactions between the 20S proteasome and its PAN/19S activators. J Biol Chem 285(1): 13-7. https://www.ncbi.nlm.nih.gov/pubmed/19889631
*denotes equal authorship