Ana Ramirez
University of Georgia, GA·Biochemistry
Parasitic infections affect more than a billion people worldwide. Many parasites coat themselves in a particular class of molecule called a glycosylphosphatidylinositol anchor, or GPI — a sugar-and-fat hybrid that sits in the cell membrane and either tethers proteins to the parasite's surface or floats there on its own.
- Fields
Biochemistry
Chemistry
Microbiology & Immunology
- Topics
glycosylphosphatidylinositol
GPI anchors
GPI-anchored proteins
- Grants
- 1 known grant, through Jun 2028
What they work on
- Establish an enzymatic pipeline that assembles the conserved glycosylphosphatidylinositol (GPI) core structure in vitro from commercially available precursors, the sugar-lipid anchor that holds proteins on the parasite cell surface.
- Screen multiple homologs of each GPI biosynthetic enzyme to identify versions with high catalytic efficiency and stability outside the cell, and optimize conditions for both single steps and multi-step one-pot reactions.
- Extend the platform with parasite-specific glycosyltransferases, the sugar-adding enzymes that create modifications absent from humans, to synthesize structurally diverse GPIs from parasites such as Plasmodium falciparum and Toxoplasma gondii.
- Generate modular GPI libraries as defined reagents for studying GPI modifications, host–pathogen interactions, and the preparation of GPI-based glycoconjugates.
More about the research
These molecules matter for getting into host cells and for steering the host's immune response. Importantly, while the central part of the GPI structure is similar across organisms, parasites decorate theirs with sugar patterns that humans do not make, which makes the parasite's GPI assembly line an attractive drug target. The obstacle is supply: the intermediates and parasite-specific GPI structures needed for laboratory experiments are very hard to synthesize chemically or purify from parasites, so the biology has been difficult to study.
Why it matters
Parasite surface anchors are promising drug targets precisely because parasites build them with sugar modifications humans lack, but research has stalled for want of pure, defined material. An enzymatic route to these molecules could supply parasite glycobiologists with standard reagents and GPI-based glycoconjugates, and could support the design of drugs aimed at parasite GPI biosynthesis in diseases such as malaria and toxoplasmosis.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Ke Hu
Arizona State University Campus Immersion, AZ·Microbiology & Immunology
Determine how the cortical microtubule array, the rib-cage-like scaffold of Toxoplasma gondii, begins its pattern at the apical polar ring, using molecular genetics, microscopy and comparative proteomics.
Thomas Sladewski
University of Connecticut, CT·Biophysics
Characterize the biophysical properties of MyoH, a Toxoplasma gondii myosin motor protein, and determine whether its force generation is required for extrusion of the conoid, the parasite's invasion organelle.
Elizabeth Egan
Stanford University, CA·Microbiology & Immunology
Determine which precise steps of Plasmodium falciparum invasion of human red blood cells require the surface proteins CD44 and CD55, using live-cell imaging and advanced microscopy of CRISPR-edited cultured red blood cells.
The school
University of Georgia: 27 labs on PI Pages, $628M a year on research, 598 research doctorates a year.
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