Beth Stadtmueller

Beth Stadtmueller

Office 412C RAL
(enter through Lab 412)

Mail to: Roger Adams Laboratory Bldg,
600 S. Mathews Avenue, MC-712 B-4
Urbana, IL 61853
Lab Page

Assistant Professor of Biochemistry

Research Topics

Host-Pathogen Interactions, Molecular Immunology, Protein Dynamics, Protein Structure, Virology

Disease Research Interests

Infectious Diseases


B.S. 2003 University of Wisconsin, Madison
Ph.D. 2010 University of Utah
Postdoc. 2011-2018 California Institute of Technology

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.

Representative Publications

Kumar Bharathkar, S.*, Parker, B. W.*, Malyutin, A. G., Haloi, N., Huey-Tubman, E. K., Tajkhorshid, E., Stadtmueller, B. M. (2020). "The structures of secretory and dimeric immunoglobulin A." Elife 9.

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]

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.

Featured “In this Issue:”

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. Featured in Caltech News:

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.

Stadtmueller, B.M. and Hill, C.P. (2011) “Proteasome Activators.” Mol Cell 41(1): 8-19.

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.

*denotes equal authorship