Joanna Slusky
University of Kansas, KS·Biochemistry
Many proteins that span the outer membrane of bacteria are shaped like barrels, with a channel running through the middle. These membrane β-barrels can act as gates that move molecules in and out of cells.
- Fields
Biochemistry
Biophysics
Computer Science
- Topics
antibiotic resistance
efflux pumps
TolC
- Grants
- 2 known grants, through Aug 2027
What they work on
- Identify sequence and structural patterns shared by peptides that bind antibiotic efflux pump-like outer-membrane barrels, using the lab's databases of membrane β-barrels and the solved helix-in-barrel structure.
- Screen for peptides that bind tightly to TolC, the outer-membrane barrel of the E. coli antibiotic efflux pump, and find the features that control binding, with the goal of plugging the pump and restoring antibiotic potency.
- Determine what allows peptides that bind TolC to be pulled through the pump, so that efflux pumps could be used to carry drugs across the bacterial outer membrane.
- Build a fold-specific protein language model that needs less training data, using a new way to restrict attention in transformer models, to learn the sequence rules of membrane β-barrels.
- Generate new barrel sequences with a patch-based 'metamorphosis' generator that redesigns one local region at a time, then test the designs as metal sensors by measuring changes in current across a membrane.
More about the research
They can also serve as frameworks that engineers redesign for new jobs. The research here studies and designs these barrels for two goals: making existing antibiotics work again against resistant bacteria, and building protein sensors that detect toxic metals in water. Both projects depend on understanding how a barrel's amino acid sequence and shape decide what binds inside it.
Why it matters
Peptides that plug the TolC efflux pump could make existing antibiotics effective again against resistant 'superbugs.' Peptides that pass through the pump could deliver drugs that normally cannot cross the bacterial outer membrane. Separately, designed protein barrels could lead to sensors for heavy-metal contaminants, supporting efforts to keep waterways clean, and the design methods could be used to build biosensors for other purposes.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Rasika Harshey
University of Texas at Austin, TX·Microbiology & Immunology
Use phage Mu transposition, which inserts DNA almost anywhere, to build a high-resolution map of contacts between genomic loci in E. coli and test how genome organization influences gene expression.
David Cafiso
University of Virginia, VA·Biophysics
Test models of how TonB-dependent transporters such as BtuB, the vitamin B12 transporter, move nutrients across the E. coli outer membrane, using site-directed spin labeling and EPR spectroscopy on active proteins.
Justin Meyer
University of California-San Diego, CA·Ecology & Evolution
Test the two-step model of how bacteriophage λ's receptor-binding protein gains new functions by finding which mutations, first destabilizing ones and then binding-loop changes, let it use new E. coli receptors, using high-throughput gene editing and phenotyping.
The school
University of Kansas: 26 labs on PI Pages, $546M a year on research, 351 research doctorates a year.
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