Justin Meyer
University of California-San Diego, CA·Ecology & Evolution
Viruses attach to host cells using receptor-binding proteins (RBPs), which latch onto specific molecules on the cell surface. Mutations in these proteins can let a virus start infecting new hosts.
- Fields
Ecology & Evolution
Microbiology & Immunology
Biochemistry
- Topics
bacteriophage lambda
phage λ
Escherichia coli
- Grants
- 1 known grant, through Apr 2030
What they work on
- 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.
- Determine which protein characteristics constrain gain-of-function evolution of the λ receptor-binding protein, and use these data to test theories of protein tradeoffs.
- Identify protein features that increase the evolvability of the receptor-binding protein, meaning its capacity to evolve new functions, and use the results to test theories of protein robustness and evolvability.
- Assemble a library of 96 E. coli outer membrane proteins and screen large receptor-binding protein variant libraries against it to measure activity across a diverse set of potential receptors.
More about the research
Many such mutations have been found, but there is still no molecular model that explains how they work well enough to predict which viruses are likely to jump hosts. The lab tackles this using bacteriophage λ (lambda), a virus that infects the bacterium Escherichia coli, a system the group has used for more than a decade to study how new functions, new species and complexity evolve.
Why it matters
A general molecular model of how viral receptor-binding proteins gain new functions could eventually help predict which viruses are likely to shift to new hosts. Such predictions could inform surveillance for emerging viral threats. The work also adds basic understanding of how new protein-protein interactions evolve and what physical principles limit or enable protein evolution.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
David Savage
University of California-Berkeley, CA·Biochemistry
Develop experimental methods to systematically map how mutations change the function of biomedically relevant proteins, such as CRISPR-Cas genome editing enzymes.
Joanna Slusky
University of Kansas, KS·Biochemistry
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.
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.
The school
University of California-San Diego: 84 labs on PI Pages, $1.9B a year on research, 637 research doctorates a year.
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