Cheryl Ingram-Smith

Assistant Professor
Genetics and Biochemistry Department

Office: 257A Life Sciences Facility
Phone: 864-656-2376


 Educational Background

Ph.D. Molecular Biology
University of Pennsylvania School of Medicine 1993

B.S. Biology
MIT 1986

 Courses Taught

BCHM 3010: Molecular Biochemistry
BCHM 3050: Essential Elements of Biochemistry
BCHM 4930: Senior Seminar
BCHM 8140: Advanced Biochemistry
BCHM/GEN 8100: Principles of Molecular Biology


Member of the Clemson University Eukaryotic Pathogens Innovation Center (EPIC) and the Clemson School of Health Research.

 Research Interests

Entamoeba histolytica is a water- and food-borne intestinal parasite of humans. Although 90% of E. histolytica infections are asymptomatic, due to its widespread prevalence in developing countries this equates to ~50 million cases of amoebic dysentery each year and as many as 100,000 deaths due to amoebic liver abscess. E. histolytica lacks many of the most common metabolic pathways present in other types of eukaryotic cells and is thought to rely on glycolysis as its main energy pathway. Glycolysis is a key pathway for the breakdown of glucose. However, E. histolytica colonizes the lower intestine where glucose levels are low, suggesting this parasite must employ other pathways for obtaining sufficient energy to infect and grow in humans. The focus of my lab is to investigate the contribution of glycolysis and other metabolic pathways to E. histolytica growth and infection. We employ a variety of biochemistry, molecular biology, genetic, and cell biology approaches to understanding this unusual and deadly organism.


T Taylor, C Ingram-Smith, and KS Smith. 2015. Biochemical and kinetic characterization of the eukaryotic phosphotransacetylase class IIa enzyme from Phytophthora ramorum. Eukaryotic Cell 14:652-660.

C Ingram-Smith*, J Wharton, C Reinholz, T Doucet, R Hesler, and KS Smith*. 2015. The role of active site residues in ATP binding and catalysis in the Methanosarcina thermophila acetate kinase. Life (Basel.) 5:861-871. (* co-corresponding authors)

C Jones and C Ingram-Smith. 2014. Biochemical and kinetic characterization of the recombinant ADP-forming acetyl-CoA synthetase from the amitochondriate protozoan Entamoeba histolytica. Eukaryotic Cell 13:1530-1537.

W Yang, C Catalanotti, S D’Adamo, TM Wittkopp, C Ingram-Smith, L Mackinder, TE Miller, AL Heuberger, G Peers, KS Smith, MC Jonikas, AR Grossman, and MC Posewitz. 2014. Alternative acetate production pathways in Chlamydomonas reinhardtii during dark anoxia and the dominant role of chloroplasts in fermentative acetate production. Plant Cell 26:4499-4518.

K Glenn, C Ingram-Smith, and KS Smith. 2014. Biochemical and kinetic characterization of xylulose 5-phosphate/fructose 6-phosphate phosphoketolase 2 (Xfp2) from Cryptococcus neoformans. Eukaryotic Cell 13:657-663.

TM Thaker, M Tanabe, M Fowler, AM Preininger, C Ingram-Smith, KS Smith, and TM Iverson. 2013. Crystal structures of acetate kinases from the eukaryotic pathogens Entamoeba histolytica and Cryptococcus neoformans. Journal of Structural Biology 181:185-189.

C Ingram-Smith*, JL Thurman*, Jr, K Zimowski, and KS Smith. 2012. Role of motif III in catalysis by acetyl-CoA synthetase. Archaea 2012:Article ID 509579. (*authors contributed equally)

ML Fowler, C Ingram-Smith, and KS Smith. 2012. Novel pyrophosphate-forming acetate kinase from the protist Entamoeba histolytica. Eukaryotic Cell 11:1249-1256.

ML Fowler, C Ingram-Smith, and KS Smith. 2011. Direct detection of the acetate-forming activity of the enzyme acetate kinase. Journal of Visualized Experimentation 58:e3474.

RD Barber, L Zhang, M Harnack, MV Olson, R Kaul, C Ingram-Smith, and KS Smith. 2011. Complete genome sequence of Methanosaeta concilii, a specialist in aceticlastic methanogenesis. Journal of Bacteriology 193:3668-3669.

Y Meng, C Ingram-Smith, LL Cooper, and KS Smith. 2010. Characterization of an archaeal medium-chain acyl-CoA synthetase from Methanosarcina acetivorans. Journal of Bacteriology 192:5982-5990.

MB Shah, C Ingram-Smith, LL Cooper, J Qu, Y Meng, KS Smith, and AM Gulick. 2009. The 2.1 Å crystal structure of an acyl-CoA synthetase from Methanosarcina acetivorans reveals an alternate acyl-binding pocket for small branched acyl substrates. Proteins 77:685-698.


Eukaryotic Pathogens Innovation Center