Qinglian Liu
Virginia Commonwealth University, VA·Biochemistry
Proteins must fold into the right shape to work. Cells rely on helper proteins called molecular chaperones to guide folding and to stop damaged proteins from clumping together.
- Fields
Biochemistry
Biophysics
Microbiology & Immunology
- Topics
molecular chaperones
Hsp70
Hsp110
- Grants
- 1 known grant, through Jun 2027
What they work on
- Determine the in vivo role of Hsp110 holdase activity (keeping unfolded proteins from clumping) in protein folding, using the selective inhibitor 2H and the genetics of the yeast Saccharomyces cerevisiae.
- Test how Hsp110 holdase activity supports protein import into the endoplasmic reticulum, and identify the natural protein substrates that Hsp110s hold in yeast cells.
- Solve the structures of Msi3, the essential Hsp110 of Candida albicans, alone and bound to 2H, to reveal how the inhibitor binds and blocks holdase activity but not nucleotide exchange.
More about the research
One essential chaperone team pairs Hsp70s with their distant relatives, Hsp110s. Hsp110s have two jobs. First, they help Hsp70s reset by swapping the energy molecule they hold, which is called nucleotide exchange factor (NEF) activity. Second, they grab unfolded proteins and keep them from clumping, which is called holdase activity. The NEF role is well understood. What the holdase role does in cells has stayed largely unknown, because no one could block it without also blocking NEF activity.
Why it matters
Fungal infections caused by Candida albicans are a serious medical problem, and doctors have limited antifungal drug options. The team's preliminary results suggest that Hsp110 chaperones may be a new drug target. The inhibitor 2H could be a starting compound for a new class of antifungals with limited toxicity to human cells. Understanding how 2H binds its target may guide the design of more selective treatments.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
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Northwestern University, IL·Biochemistry·Early-career
Determine how IRE1, an ER stress sensor, physically connects to the protein-making translational machinery, using single-particle cryo-electron microscopy to resolve the 3D structures involved.
Raquel Lieberman
Georgia Institute of Technology, GA·Biochemistry
Screen the baker's yeast gene-deletion library for strains that survive toxic mutant myocilin, to find cellular pathways that make cells vulnerable to this glaucoma protein.
Karen Norris
University of Georgia, GA·Microbiology & Immunology
Test whether the NXT-2 vaccine, a lab-made peptide based on a fungal protein shared across species, triggers strong immune responses in nonhuman primates.
The school
Virginia Commonwealth University: 19 labs on PI Pages, $524M a year on research, 438 research doctorates a year.
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