# Essential function of a putative glycosyltransferase in P. falciparum

> **NIH NIH R21** · UNIVERSITY OF GEORGIA · 2022 · $226,500

## Abstract

Project Summary
The lethal form of human malaria is caused by the intracellular parasite Plasmodium falciparum, which
causes nearly 450,000 deaths every year. Infection by these parasites results in ~250 million infections
each year. However, there are no effective vaccines against malaria and the parasite has gained
resistance to all antimalarial drugs used in the clinic. Further, these drug-resistant strains are spreading
throughout the world. Therefore, it is crucial to identify essential druggable pathways used by the parasite
to grow within human host cells. One such poorly understood but essential pathway is the modification
of parasite proteins by sugar molecules or glycans. In other model organisms, this process is essential
for protein function and mostly occurs in the secretory pathway. Recent work in Plasmodium parasites
has shown that glycan modification of several parasite surface ligands play an essential role in parasite
transmission and its development within the mosquito vector. But little is known about the function, if any,
of glycosylation during the clinically important intraerythrocytic growth of P. falciparum. We recently
identified a putative glycosyltransferase as an essential interactor of a heat shock protein residing in the
endoplasmic reticulum. To study its function during the intraerythrocytic stages of parasite growth, we
generated conditional mutants for this protein. We hypothesize that the glycosyltransferase function of
this protein plays an essential function during intraerythrocytic growth of P. falciparum. Our preliminary
data show that this protein is essential for parasite growth within human red blood cells and is required
for the egress of daughter parasites from the host cell at the end of the intraerythrocytic life cycle. Using
cellular, biochemical, and genetic approaches, we will define the function of this gene during egress of
daughter parasites. The essentiality of the putative glycosyltransferase activity for parasite survival will
be tested. The proposed studies will use recombinant enzyme to define the enzymatic activity of this
glycosyltransferase. Proximity-dependent biotinylation approaches combined with mass spectrometry
will be used to identify interactors as well as putative substrates. The success of this project will reveal
novel and essential glycosylation pathways used by the parasite for asexual expansion in human red
blood cells.

## Key facts

- **NIH application ID:** 10382321
- **Project number:** 5R21AI153851-02
- **Recipient organization:** UNIVERSITY OF GEORGIA
- **Principal Investigator:** Vasant Muralidharan
- **Activity code:** R21 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2022
- **Award amount:** $226,500
- **Award type:** 5
- **Project period:** 2021-04-05 → 2024-03-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/10382321

## Citation

> US National Institutes of Health, RePORTER application 10382321, Essential function of a putative glycosyltransferase in P. falciparum (5R21AI153851-02). Retrieved via AI Analytics 2026-06-01 from https://api.ai-analytics.org/grant/nih/10382321. Licensed CC0.

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