Niraj H. Tolia, Ph.D.

Associate Professor
Molecular Microbiology

Molecular Microbiology and Microbial Pathogenesis Program
Biochemistry, Biophysics, and Structural Biology Program

  • (314) 286-0134

  • (314) 286-0164

  • (314) 362-1232

  • 8230

  • Rm 8230, McDonnell Pediatric Research Building



  • biochemistry, biophysics, parasitology, microbiology, malaria, protein-protein interaction, protein crystallography, structural biology, pathogenesis

  • The pathogenesis of infectious disease from atom to host-pathogen interaction

Research Abstract:

The Tolia Laboratory study the pathogenesis of infectious disease from atom to host-pathogen interaction

We use the tools of structural biology, biochemistry, biophysics, and microbiology to examine proteins and protein complexes associated with pathogenesis.

One major focus is to define the molecular mechanisms required for the pathogenesis of malaria. Malaria affects half the world`s population, leads to 300-500 million cases per year, and results in approxiamately 1 million deaths annually. A majority of fatalities are in children under the age of five.

A second major focus is to define the mechanisms of bacterial drug resistance to available antibiotics. Drug resistance has emerged as a major global threat to the control of previously routine infections.

We pursue four areas of research:
- Host-pathogen interactions
- Neutralizing antibodies
- Antigen engineering
- Drug resistance

Selected Publications:

Park J, Gasparrini AJ, Reck MR, Elliott JL, Vogel JP, Wencewicz TA, Dantas G, Tolia NH. “Structural basis for plasticity and inhibition of emerging tetracycline resistance enzymes” Nature Chemical Biology (2017) Jul;13(7):730-736.

Jimah JJ, Salinas ND, Sala-Rabanal M, Jones NG, Sibley LD, Nichols C, Schlesinger P, Tolia NH. “Malaria parasite CelTOS targets the inner leaflet of cell membranes for pore-dependent disruption” Elife (2016) Dec 1;5. pii: e20621. doi: 10.7554/eLife.20621.

Chen E, Salinas ND, Huang Y, Ntumngia F, Plasencia MD, Gross ML, Adams JH, Tolia NH. “Broadly neutralizing epitopes in the Plasmodium vivax vaccine candidate Duffy Binding Protein” Proceedings of the National Academy of Sciences USA (2016) May 31; 113(22):6277-82.

Chen E, Salinas ND, Ntumngia FB, Adams JH, Tolia NH. "Structural analysis of the synthetic Duffy Binding Protein (DBP) antigen DEKnull relevant for Plasmodium vivax malaria vaccine design." PLOS Neglected Tropical Diseases (2015) Mar 20;9(3):e0003644

Salinas ND, Paing MM, Tolia NH. "Critical glycosylated residues in exon three of erythrocyte glycophorin A engage Plasmodium falciparum EBA-175 and define receptor specificity." mBio (2014) 5(5):01606-14.

Guggisberg AM#, Park J#, Edwards RL, Kelly ML, Hodge DM, Tolia NH*, Odom AR*. "A sugar phosphatase regulates the methylerythritol phosphate (MEP) pathway in malaria parasites." Nature Communications (2014) 5:4467. # co-first author, * co-senior author

Batchelor JD, DeKoster GT, Henzler-Wildman KA, Tolia NH. “Red blood cell invasion by Plasmodium vivax: Structural basis for DBP engagement of DARC” PLoS Pathogens (2014) Jan;10(1):e1003869.

Chen E, Paing MM, Salinas ND, Sim BK, Tolia NH. “Structural and functional basis for inhibition of erythrocyte invasion by antibodies that target Plasmodium falciparum EBA-175” PLoS Pathogens (2013) 9(5):e1003390.

Malpede BM, Lin DH, Tolia NH. “Molecular basis for sialic acid-dependent receptor recognition by Plasmodium falciparum Erythrocyte Binding Antigen 140” Journal of Biological Chemistry (2013) Apr 26;288(17):12406-15.

Batchelor JD, Zahm JA, Tolia NH. Dimerization of Plasmodium vivax DBP is induced upon receptor binding and drives recognition of DARC. Nature Structural and Molecular Biology (2011) Jul 10;18(8):908-14.

Last Updated: 9/15/2017 10:47:07 AM

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