Publications
- S. L. De, S. May, K. Shah, M. Slawinski, S. Changrob, S. Xu, S. J. Barnes, P. Chootong, F. B. Ntumngia, J. H. Adams. "Variable immunogenicity of a vivax malaria blood-stage vaccine candidate". Vaccine, 39(19), 2668–2675. (2021) (link)
- S. May, C. Climent, Z. Tao, S. A. Vinogradov, J. E. Subotnik. "Spin-orbit versus Hyperfine Coupling Mediated Intersystem Crossing in a Radical Pair". J. Phys. Chem. A. Accepted, jp-2023-00294x.R1 (2023) (2023)
Research Experience
- Helpful overview in poster form
- Dr. John Adams
- Chen E, Salinas ND, Ntumngia FB, Adams JH, Tolia NH. (2015). Structural analysis of the synthetic Duffy Binding Protein (DBP) antigen DEKnull relevant for Plasmodium vivax malaria vaccine design. PLoS Negl Trop Dis. 9(3): e0003644.
- Chen E, Salinas ND, Huang Y, Ntumngia F, Plasencia MD, Gross ML, Adams JH, Tolia NH (2016). Broadly neutralizing epitopes in the Plasmodium vivax vaccine candidate Duffy Binding Protein. Proc Natl Acad Sci. 113(22):6277-82.
- Ntumngia, F.B*, Chootong, P*, VanBuskirk, KM*, Xainli, J, Cole-Tobian, JL, Campbell, CO, Fraser, TS, King, CL, Adams, JH (2010). Mapping epitopes of the Plasmodium vivax Duffy binding protein with naturally acquired inhibitory antibodies. Infection and Immunity. 78(3):1089-95.
- Ntumngia FB, Schloegel J, Barnes SJ, McHenry AM, Singh S, King CL, and Adams JH. (2012). Conserved and variant epitopes of Plasmodium vivax Duffy binding protein as targets of inhibitory monoclonal antibodies. Infection and Immunity. 80(3):1203-1208.
Research assistant in the Dr. Adams Lab (2018-2019)
I studied P. Vivax's DBPII protein under Dr. Sai Lata De at the University of South Florida. This was a formative foray into everything molecular biology, including mammilian cell cultures, transfection, transformation, PCR, flow cytometry, and basic immunologic assays like ELISAs and western blots.
My project dealt with characterizing the effects of different variables on the immunigenicity of DBPII in both wild type and inbred mouse models. This research was inspired by previous work by Dr. Francis Ntumngia and others, and centers around DBPII's highly conserved nature and its ability to elicit high-titre inhibitory antibodies.
The reason for DBPII's highly conserved nature can be attributed to its function in the P. vivax parasite. P. vivax preferentially invades reticulocytes (young red blood cells) via binding between PvDBP and the reticulocyte's Duffy antigen receptor for chemokines (DARC). Region II of the DBP protein (DBPII) contains critical residues for heterotetramer formation when P. vivax invades the reticulocyte. Because of these critical residues, DBPII is a natural vaccine target.
Inhibitory antibodies are a subset of antibodies that block a protein's active site, therefore inhibiting its function. This makes them especially desirable for vaccine design, as they can block critical antigens on a given pathogen. To evaluate the degree to which anti-DBPII mouse antibodies blocked DBPII-DARC heterotetramer formation, we used an in vitro inhibition assay. Cos7 cells were transiently transfected with DPII_GFP and were incubated in anti-DBPII mouse serum. The cells were then incubated in human erythrocytes to evaluate neutralization of the DBPII expressed on the surface of Cos7 cells. When functional inhibition of the mouse sera sample is lower, more "rosettes" (Cos7 cell covered in erythrocytes, shown below) will be observed.
Further reading and info
More photos
Undergraduate in the Dr. Tomson Lab (2020-2021)
I'm currently putting together a summary of research with Dr. Tomson.Undergraduate in Subotnik lab (2021-present)
Surface hopping, electrochemistry simulations, hyperfine coupling/radical pairs, EPR simulations, oh my! (currently compiling research to date).Qchem