Niraj H. Tolia, Ph.D.

Associate Professor
Molecular Microbiology

Molecular Microbiology and Microbial Pathogenesis Program
Biochemistry Program

  • (314) 286-0134

  • (314) 286-0164

  • (314) 362-1232

  • 8230

  • Rm 8230, McDonnell Pediatric Research Building

  • tolia@wustl.edu

  • http://tolialab.wustl.edu

  • 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:

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. # co-first author

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

Paing MM, Tolia NH “Multimeric assembly of host-pathogen adhesion complexes involved in apicomplexan invasion” PLoS Pathogens (2014) 10(6): e1004120.

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.

Salinas ND, Tolia NH. “A quantitative assay for binding and inhibition of Plasmodium falciparum Erythrocyte Binding Antigen 175 reveals high affinity binding depends on both DBL domains” Protein Expression and Purification (2014) Mar;95:188-94.

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.

Lin DH, Malpede BM, Batchelor JD, Tolia NH. Crystal and Solution Structures of Plasmodium falciparum Erythrocyte Binding Antigen 140 Reveal Determinants of Receptor Specificity during Erythrocyte Invasion. Journal of Biological Chemistry (2012) Oct 26;287(44):36830-6.

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: 3/14/2016 4:12:12 PM

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