I have always been interested in science — beginning with fossil hunting and bird watching with my father, a scientist involved in multiple fields of study. In graduate school, I fell in love with X-ray crystallography. This technique allows us to “zoom in” to see protein structures in atomic detail, almost as if you could enlarge a protein sufficiently to hold it between your hands and stare at it.
My lab uses the tools and techniques of structural biology and biophysical chemistry to understand the function of proteins involved in microbial pathogenesis and host immune response. We are particularly interested in the molecular mechanisms underlying the formation of staphylococcal biofilms, which are specialized colonies of bacteria that are highly resistant to antibiotics or immune responses. We are also studying several immune pathways involving antibody-receptor interactions, immune signaling and immune trafficking.
Our broad goals are to understand how key proteins function to either promote infection by pathogens, such as staphylococcus bacteria, or how they facilitate the host's immune responses to a pathogen. We are always interested in using these insights to develop novel therapeutic agents.
My lab discovered the mechanism by which staphylococcal bacteria stick to one another in a biofilm. They have long, filament-like proteins that become sticky in the presence of zinc ions, creating twisted rope-like structures between the cells. We found that by removing the available zinc ions with a chelator, we could inhibit biofilm growth. This discovery led to the development of a novel antimicrobial platform that is entering clinical trials later this year.
In 2014, I was awarded the Emerging Entrepreneurial Achievement Award from the University of Cincinnati. This award was based on our work to develop and commercialize the BioLexa antimicrobial platform. I have been a researcher for more than 17 years, and I began my work at Cincinnati Children's in 2014.
BA: Oral Roberts University, Tulsa, OK, 1993.
PhD: Washington University Medical School, St. Louis, MO, 1999.
Postdoc: California Institute of Technology, Pasadena, CA, 2003.
Structural biology and biophysics of antibodies; immune receptors; bacterial surface proteins
Immunobiology, Infectious Diseases
Solution Structural Studies of Pre-amyloid Oligomer States of the Biofilm Protein Aap. Journal of Molecular Biology. 2022; 434:167708.
Pregnancy enables antibody protection against intracellular infection. Nature. 2022; 606:769-775.
Biofilm propensity of Staphylococcus aureus skin isolates is associated with increased atopic dermatitis severity and barrier dysfunction in the MPAACH pediatric cohort. Allergy: European Journal of Allergy and Clinical Immunology. 2021; 76:302-313.
The staphylococcal biofilm protein Aap forms a tetrameric species as a necessary intermediate before amyloidogenesis. The Journal of biological chemistry. 2020; 295:12840-12850.
The biofilm adhesion protein Aap from Staphylococcus epidermidis forms zinc-dependent amyloid fibers. The Journal of biological chemistry. 2020; 295:4411-4427.
FcαRI binding at the IgA1 CH2-CH3 interface induces long-range conformational changes that are transmitted to the hinge region. Proceedings of the National Academy of Sciences of USA. 2018; 115:E8882-E8891.
Functional consequences of B-repeat sequence variation in the staphylococcal biofilm protein Aap: deciphering the assembly code. The Biochemical journal. 2017; 474:427-443.
Structural basis for collagen recognition by the immune receptor OSCAR. Blood. 2016; 127:529-537.
IgG1 protects against renal disease in a mouse model of cryoglobulinaemia. Nature. 2015; 517:501-504.
Structural basis for Zn2+-dependent intercellular adhesion in staphylococcal biofilms. Proceedings of the National Academy of Sciences of USA. 2013; 110:E202-E211.
Andrew B. Herr, PhD8/30/2024