Research in the Muralidharan lab is aimed at understanding the biology of Plasmodium, the deadly human parasite that causes malaria. It is a disease that afflicts nearly 500 million people and causes almost a million deaths each year. Our goal is to uncover the molecular mechanisms that drive the parasitic life cycle of Plasmodium. The aim of this research is to leverage our knowledge of parasite biology towards development of intervention strategies that disrupt the disease process. We deploy a wide variety of tools to study the parasite including CRISPR/Cas9 genome engineering, cellular biology, chemical biology, molecular biology and biochemistry.
Our research focuses on organelle biology in this deeply branched eukaryote. We are particularly interested in the biology of the endoplasmic reticulum and the four-membrane plastid known as the apicoplast. The ER of Plasmodium is the start of a complex and highly branched protein trafficking pathway. The apicoplast is a unique parasite-specific organelle that provides essential metabolic pathways to these organisms.
- Muralidharan V., Oksman A., Pal P., Lindquist S. and Goldberg D. E. (2012)Plasmodium falciparum Hsp110 stabilizes the Asn repeat-rich parasite proteome during malarial fevers. Nat. Commun., 3:1310 (doi:10.1038/ncomms2306)
- Muralidharan V., Oksman A., Iwamoto M., Wandless T.J. and Goldberg D. E. (2011) Aspragine repeat function in a Plasmodium falciparum protein assessed via a regulatable fluorescent affinity tag. Proc. Natl. Acad. Sci. USA, 108,4411-4416.
- Russo I., Babbit S.*, Muralidharan V.*, Butler T., Oksman A. and Goldberg D. E. (2010). Plasmepsin V Licenses Plasmodium Proteins for Export Into the Host Erythrocyte. Nature ,463, 632-636
- Cho J.H., Muralidharan V., Vila-Perello M., Raleigh D.P., Muir T.W. and Palmer III A.G. (2011) Tuning Protein Autoinhibition by Domain Destabilization. Nat. Struc. Mol. Biol., 18, 550-555.
- Muralidharan V.*, Dutta K.*, Cho J. H., Vila-Perello M., Raleigh D. P., Cowburn D. and Muir T. W. (2006). Solution Structure and Folding Characteristics of the C-terminal SH3 Domain of c-Crk-II. Biochemistry, 45, 8874-88
- Muralidharan V. and Muir T. W. (2006). Protein Ligation: An Enabling Technology for the Biophysical Analysis of Proteins. Nat. Methods, 3, 429-438
- Muralidharan V., Cho J. H., Trester-Zedlitz M., Kowalik L., Chait B. T., Raleigh D.P., and Muir T. W. (2004). Domain-specific Incorporation of Noninvasive Optical Probes into Recombinant Proteins. J. Am. Chem. Soc., 126, 14004-14012