The Division of Molecular Microbiology conducts basic and applied research related to bacterial, parasitic and viral diseases that are of major public health concern. Our research is focused to two broad areas:

Our major topics of interest include HIV, tuberculosis, malaria, mechanisms of antimicrobial resistance, enteric diseases, toxins, and diagnostics. Student training and development are integral components of faculty research.

Division Faculty

    Dr. Salvador Almagro-Moreno
  • Title: Assistant Professor
  • Office: BMS 125A
  • Phone: 407.823.3982; 407.823.3987 (lab)
  • Emergence and Evolution of Bacterial Pathogens
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  • Biography:

    Our primary scientific interest lies at the interface between ecology and pathogenesis. We investigate how environmental factors affect the pathogenic potential of marine bacteria, which genetic traits are prerequisites in colonizing a new niche such as the human host, how they acquire and regulate virulence genes, and what are their ecological relationships with other members of their natural environment and the host’s microbiota.

    We study members of the family Vibrionaceae, a highly diverse group of marine bacteria that includes from symbionts to human pathogens. Some of the species we work with include Vibrio cholerae, the etiological agent of the severe diarrheal disease cholera, Vibrio vulnificus, an emergent pathogen that causes a deadly septicemia, and Vibrio coralliilyticus, a coral pathogen whose emergence is linked to climate change.

    Our research approach strives to be holistic and multidisciplinary; what we call “From Bays to Bases”. It encompasses a mix of molecular biology, genomics, phylogenetics, pathogenesis, and ecology. We believe that by understanding pathogen evolution and ecology we will ultimately gain the knowledge that will allow us to forecast the traits of emergent virulent strains, predict the sources of outbreaks, and to design and produce affordable and safe vaccines and reliable treatments against bacterial threats.

    Learn more about my lab atwww.vibriocholerae.org

    Recent Publications

     

    1. Bile salts and alkaline pH reciprocally modulate the interaction between the periplasmic domains of Vibrio cholerae ToxR and ToxS
    C. R. Midgett, S. Almagro-Moreno, M. Pellegrini, R. K. Taylor, K. Skorupski, F. J. Kull. Molecular Microbiology. 2017

    2. Origins of pandemic clones from environmental gene pools
    B. J. Shapiro, I. Levade, G. Kovacikova, R. K. Taylor, S. Almagro-Moreno*. Nature Microbiology. 2016

    3. Intestinal colonization dynamics of Vibrio cholerae
    S. Almagro-Moreno*, K. Pruss, and R. K. Taylor. PLoS Pathogens. 2015

    4. Proteolysis of virulence regulator ToxR is associated with entry of Vibrio cholerae into a dormant state
    S. Almagro-Moreno*, T. K. Kim, K. Skorupski, and R. K. Taylor. PLoS Genetics. 2015

    5. Role of ToxS in the proteolytic cascade of virulence regulator ToxR in Vibrio cholerae
    S. Almagro-Moreno*, M. Z. Root, and R. K. Taylor. Molecular Microbiology. 2015

    6. Host-like carbohydrates promote bloodstream survival of Vibrio vulnificus in vivo
    J. B Lubin, W. G. Lewis, N. M. Gilbert, S. Almagro-Moreno, E. F. Boyd, A. L. Lewis. Infection and Immunity. 2015

    7. Cholera: Environmental reservoirs and impact on disease transmission
    S. Almagro-Moreno and R. K. Taylor. Microbiology Spectrum. 2013

    8. Cholera: Environmental reservoirs and impact on disease transmission
    S. Almagro-Moreno and R. K. Taylor. Book chapter for “OneHealth: People, Animals, and Environment”. ASM press. 2013

    9. Ecology and genetic structure of a northern temperate Vibrio cholerae population related to toxigenic isolates
    B. M. Schuster, A. L. Tyzik, R. A. Donner, M. J. Striplin, S. Almagro-Moreno, S. H. Jones, V. S. Cooper, and C. A. Whistler. Applied Environmental Microbiology. 2011

    10. An atomic force microscopy method for the detection of binding forces between bacteria and a lipid bilayer containing higher order gangliosides
    E. L. Adams, S. Almagro-Moreno and E. F. Boyd. Journal of Microbiological Methods. 2010

    11. Dichotomy in the evolution of pathogenicity island and bacteriophage encoded integrases from pathogenic Escherichia coli strains
    S. Almagro-Moreno, M. G. Napolitano and E. F. Boyd. Infection, Genetics and Evolution. 2010

    12. Excision dynamics of Vibrio pathogenicity island-2 from Vibrio cholerae: role of a recombination directionality factor VefA
    S. Almagro-Moreno, M. G. Napolitano and E. F. Boyd. BMC Microbiology. 2010

    13. Bacterial catabolism of nonulosonic (sialic) acid and fitness in the gut
    S. Almagro-Moreno and E. F. Boyd. Gut Microbes. 2010

    14.. How genomics has shaped our understanding of the evolution and emergence of pathogenic Vibrio cholerae
    S. Almagro-Moreno, R. Murphy, and E. F. Boyd. Book chapter for “Genomics of Foodborne and Waterborne Pathogens“. ASM press, 2010

    15. Sialic acid catabolism confers a competitive advantage to pathogenic Vibrio cholerae in the mouse intestine
    S. Almagro-Moreno and E. F. Boyd. Infection and Immunity. 2009

    16. Insights into the evolution of sialic acid catabolism among bacteria
    S. Almagro-Moreno and E. F. Boyd. BMC Evolutionary Biology. 2009

    17. Genomic islands are dynamic, ancient integrative elements in bacterial evolution
    E. F. Boyd, S. Almagro-Moreno and M. A. Parent. Trends in Microbiology. 2009

    18. The genomic code: inferring Vibrionaceae niche specialization
    F. J. Reen, S. Almagro-Moreno, D. Ussery and E. F. Boyd. Nature Reviews Microbiology.2006

     

    *Corresponding author

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    Dr. Debopam Chakrabarti
  • Title: Professor & Molecular Microbiology Division Leader
  • Office: Biomedical Research Annex (BRA) 140
  • Phone: 407.882.2256
  • Studies molecular mechanisms of the intraerythrocytic life cycle of the malaria parasite, Plasmodium falciparum, and discovery of antimalarials from natural products and natural product-like synthetic compounds.
  • Send an Email
  • Biography:

    Malaria afflicts about half of the world population causing over 500,000 deaths each year. In addition to contributing significantly towards overall childhood mortality in the poorest nations, the disease is estimated to cause considerable reductions in the economic growth of countries that bear a heavy malaria burden. The situation is made worse because the widespread prevalence of drug resistant parasites is rendering the limited number of available drugs less and less effective for clinical use. Therefore, there is a pressing need for novel therapeutic options to treat multidrug resistant malaria. It is also important to understand the molecular mechanism of parasite growth and differentiation so that novel therapeutic targets can be identified.

    A major focus of research in my laboratory is to identify next generation of antimalarial compounds from unique areas of medicinally relevant chemical space. To pursue this goal we are engaged in screening focused libraries of natural product-based synthetic compounds as well as natural product extracts from under explored marine biodiversity and fungi.  Our research has discovered many novel scaffolds with potent and selective antiplasmodial activities with cellular action distinct from current antimalarials, including one that cures malaria in the rodent model. Another aspect of research in my laboratory focuses on understanding molecular mechanisms of the intraerythrocytic life cycle of the malaria parasite, Plasmodium falciparum. Specifically, we are engaged in defining precise physiological roles of Plasmodium protein kinases that are key regulators of its complex developmental stages through identification of their substrates. We recently performed isobaric tag-based quantitative proteomics and phosphoproteomics analyses of three developmental stages in the Plasmodium asexual cycle. Our system-wide comprehensive analysis is a major step towards elucidation of kinase-substrate pairs operative in various signaling networks in the parasite. This rich dataset will be useful in defining and targeting the parasite’s signaling network. Many of the unique features of parasite protein kinases can potentially be exploited to design new generation of malaria therapeutics.

    Recent Publications

    1. Roberts, B.F., Iyamu, I.D., Lee, S., Lee, E., Ayong, L., Kyle, D.E., Yuan, Y., Manetsch, R., Chakrabarti, D. (2016) Spirocyclic chromanes exhibit antiplasmodial activities and inhibit all intraerythrocytic life cycle stages. Int. J. Parasitol. Drugs Drug Resist. 6, 85-92.
    2. Chakrabarti, D. and Wright, A. (2015) Anti-malarial compounds from marine natural compounds. US Patent: 9,181,251 B2. Nov 10, 2015.
    3. Arora, S., Mauser, J., Chakrabarti, D., Schulte, A. (2015) Spatially resolved micro-absorption spectroscopy with a broadband source and confocal detection. Optics Communication, 355, 533-537.
    4. Koyama, F.C., Azevedo, M.F., Budu, A., Chakrabarti, D., Garcia, C.R. (2014) Melatonin-induced upregulation of gene expression related to ubiquitin/proteasome system in human malaria parasite Plasmodium falciparum. Int. J. Mol. Sci. 15, 22320-30.
    5. Pease, B., Huttlin, E., Jedrychowski, M.P., Talevich, E., Harmon, J., Dillman, T., Kannan, N., Doerig, C., Chakrabarti, R., Gygi, S., Chakrabarti, D. (2013) Global analysis of protein expression and phosphorylation of three stages of Plasmodium falciparum intraerythrocytic development. J. Proteome. Res. 12, 4028-45.
    6. Alvarado, S. Roberts, BF, Wright, A.E., Chakrabarti, D. (2013) The bis(indolyl)imidazole alkaloid nortopsentin A exhibits antiplasmodial activity. Antimicrob Agents Chemother 57, 2362-64.
    7. Dorin-Semblat, D., Carvalho, T. G., Nivez, M-P.,Goldring, D., Chakrabarti, D., Dhar, S., Goldberg, D., Tilley, L., Doerig, C. (2013) An atypical cyclin-dependent kinase controls Plasmodium falciparum proliferation rate. Kinome 1, 4-16.
    8. Koyama, F.C., Ribiero, R.Y., Garcia, J.L. Chakrabarti, D., and Garcia, C.R. (2012) Ubiquitin proteasome system and the atypical kinase PfPK7 are involved in melatonin signaling in Plasmodium falciparum . J. Pineal Res. 53, 147-53.
    9. Dorin-Semblat, D., Goldring, D., Patterson, S., Quashie, N., Reininger, L., Schmitt, S., Meijer, L., Chakrabarti, D., and Doerig, C. (2011) Plasmodium falciparum NIMA-related kinase Pfnek-1: sex-specificity, essentiality for the erythrocytic asexual cycle. Microbiology 157, 2785-94.
    10. Ayong, L., Da Silva, T., Mauser, J., Allen, C.A., Chakrabarti, D. (2011) Evidence for prenylation-dependent targeting of a Ykt6 SNARE in Plasmodium falciparum. Mol. Biochem. Parasitol. 175, 162-8.
    11. Halbert, J., Ayong, L., Equinet, L., Le Roch, K., Hardy, M., Goldring, D., Chakrabarti, D., Reininger, L., Doerig, C. (2010) A Plasmodium falciparum transcriptional cyclin-dependent kinase-related kinase with a crucial role in parasite proliferation associates with histone deacytylase activity. Eukaryot. Cell 9, 952-9.
    12. Davoodi-Semiromi A., Schreiber, M., Nalapalli, S., Verma, D., Singh, N. D, Banks, R. K., Chakrabarti, D., Daniell, H. (2010) Chloroplast-derived vaccine antigens confer dual immunity against cholera and malaria by oral and injectable delivery. Plant Biotechnol. J., 8, 223-48.
    13. Ayong, L., Raghavan, A., Schneider, T.G., Taraschi, T. F., Fidock, D. A., Chakrabarti, D. (2009). The longin domain regulates the steady state dynamics of Sec 22 in Plasmodium falciparum. Eukaryot. Cell, 8, 1330-40.
    14. Koyama, F.C., Chakrabarti, D., Garcia C. R. (2009) Molecular Machinery of signal transduction and cell cycle regulation in Plasmodium. Mol. Biochem. Parasitol. 165, 1-7.
    15. Chakrabarti, D. (2009). A methods-based biotechnology course for undergraduates. Biochem. Mol. Biol. Educ. 37, 227-31.
    16. Chakrabarti, R., Chakrabarti, D. (2009) Chemotherapeutics of neglected waterbourne parasites: current status and future perspectives. Mol. Cell. Pharmacol. 1, 98-102.

     

    For more publication information, please visit Pubmed.

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    Dr. Alexander M. Cole
  • Title: Professor
  • Office: BMS 236A
  • Phone: 407.823.3633
  • Studies host defense of human mucosal surfaces, with particular emphasis on Staphylococcus aureus nasal carriage, and HIV transmission and pathogenesis.
  • Send an Email
  • Biography:

    For the past two decades, Dr. Cole has been investigating an increasingly important aspect of the human immune system called “innate host defense”, which is involved in the body’s immediate response to germs such as viruses and bacteria. The main pathogenic virus that he studies is HIV (human immunodeficiency virus), which can cause the disease AIDS (acquired immunodeficiency syndrome). Worldwide, the majority of new HIV infections are in women who contracted the virus through sexual contact, which has prompted Dr. Cole to study women’s health aspects that lead to HIV transmission. Additionally, his lab is interested in developing prophylactic drugs called “microbicides” that can prevent or limit sexually transmitted HIV. A new microbicide that his lab has developed is currently being tested to confirm that it is safe and effective against HIV.

    Dr. Cole also studies how the bacterium Staphylococcus aureus, or “Staph”, can colonize the inside of human noses and be transmitted to other people. While Staph is essentially harmless to a person’s nose, that nose serves as a major reservoir for transmitting Staph and causing serious disease. Since this bacterium alone accounts for more deaths in the U.S. than HIV/AIDS, and many Staph are resistant to the majority of available antibiotics, it is evermore important to understand how humans can harbor this bacterium in their noses and to develop new drugs to kill Staph. Both of these aspects are being actively pursued in Dr. Cole’s laboratory.

    Recent Publications

    1. Sivaraman, K., A.M. Cole. (2009). Pathogenesis gene families in the common minimal genome of Staphylococcus aureus are hypervariable. FEBS Letters. 583(8): 1304-8. (PMCID: PMC2677416)
    2. Martellini, J.A., A.L. Cole, N. Venkataraman, G.A. Quinn, P. Svoboda, B.K. Gangrade, J. Pohl, O.E. Sørensen, and A.M. Cole. (2009). Cationic polypeptides are major anti-HIV-1 factors in human seminal plasma. FASEB J. 23(10): 3609-18. NIHMS# 219133
    3. Quinn, G.A., P.M. Tarwater, and A.M. Cole. (2009). Subversion of IL-1-mediated host defense by a nasal carrier strain of Staphylococcus aureus. Immunology. 128: e222-229. (PMCID:  PMC2753939)
    4. Venkataraman, N., A.L. Cole, P. Ruchula, A.J. Waring, R.I. Lehrer, O. Stuchlik, J. Pohl, and A.M. Cole. (2009). Reawakening retrocyclins:  ancestral human theta-defensins with activity against HIV-1. PLoS Biology. 7(4): e95. (PMCID: PMC2672613). (received Editor’s pick, and was selected for a commissioned synopsis)
    5. Cole, A.M., D.L. Patton, L.C. Rohan, A.L. Cole, Y. Cosgrove-Sweeney, N.A. Rogers, D. Ratner, A. Sassi, P. Tarwater, B. Ramratnam, P. Ruchala, R.I. Lehrer, A.J. Waring, and P. Gupta. (2010). The formulated microbicide RC-101 was safe and antivirally active following intravaginal application in pigtailed macaques. PLoS ONE. 5(11): e15111. (PMCID: PMC2993972)
    6. Micewicz E.D., A.L. Cole, C.L. Jung, H. Luong, M.L. Phillips, P. Pratikhya, S. Sharma, A.J. Waring, A.M. Cole, and P. Ruchala. (2010). Grifonin-1: a small HIV-1 entry inhibitor derived from the algal lectin, Griffithsin. PLoS ONE. 5(12): e14360. (PMCID: PMC3002932)
    7. Lamers, R.P., J.W. Stinnett, G. Muthukrishnan, C.L. Parkinson, and A.M. Cole. (2011). Evolutionary analyses of Staphylococcus aureus reveal that human nares harbor strains responsible for community- and hospital-acquired infections. PLoS ONE 6(1): e16426. (PMCID: PMC3025037)
    8. Martellini, J.A., A.L. Cole, P. Svoboda, O. Stuchlik, L.M. Chen, K.X. Chai, B.K. Gangrade, O.E. Sørensen, J. Pohl, and A.M. Cole. (2011). HIV-1 enhancing effect of prostatic acid phosphatase peptides is reduced in human seminal plasma. PLoS ONE. 6(1): e16285. (PMCID: PMC3024420)
    9. Sassi, A.B., M.R. Cost, A.L. Cole, A.M. Cole, D.L. Patton, P. Gupta and L.C. Rohan. (2011). Formulation development of Retrocyclin-1 (RC-101) as an anti-HIV vaginal microbicide product. Antimicrob Agents Chemother. 55(5): 2282-9. (PMCID: PMC3088226)
    10. Muthukrishnan, G., G.A. Quinn, R.P. Lamers, C. Diaz, A.L. Cole, S. Chen, and A.M. Cole. (2011). Exoproteome of Staphylococcus aureus reveals putative determinants of nasal carriage. J Proteome Res. 10(4): 2064-78. (PMCID:  PMC3070068)
    11. Sassi, A.B., K.E. Bunge, B.L. Hood, T.P. Conrads, A.M. Cole, P. Gupta, and L.C. Rohan. (2011). Preformulation and stability in biological fluids of the retrocyclin RC-101, a potential anti-HIV topical microbicide. AIDS Res Ther. 8(27): (Epub ahead of print). (PMCID: PMC3199744)
    12. Lamers, R.P., C.R. Eade, A.J. Waring, A.L. Cole, and A.M. Cole. (2011). Characterization of the retrocyclin analogue RC-101 as a preventative of Staphylococcus aureus nasal colonization. Antimicrob Agents Chemother. 55(11): 5338-46. (PMCID: PMC3195007)
    13. Ruchala, P., S. Cho, A.L. Cole, C. Carpenter, C.L. Jung, H. Luong, E.D. Micewicz, A.J. Waring, A.M. Cole, B.C. Herold, and R.I. Lehrer. (2011). Simplified theta-defensins: search for new antivirals. Int J Pept Res Ther. 17(4): 325-336.
    14. Li, M., D.L. Patton, Y. Cosgrove-Sweeney, D. Ratner, L.C. Rohan, A.M. Cole, P. Tarwater, P. Gupta, and B. Ramratnam. (2011). Incorporation of the HIV-1 microbicide cyanovirin-N in a food product. J AIDS. 58(4): 379-384. (PMCID: PMC3440868)
    15. Levinson, P., R.Y. Choi, A.L. Cole, T. Hirbod, S. Rhedin, B. Payne, B. Guthrie, R. Bosire, A.M. Cole, C. Farquhar, and K. Broliden. (2012). HIV-neutralizing activity of cationic polypeptides in cervicovaginal secretions of women in HIV-serodiscordant relationships. PLoS ONE. 7(2): e31996. (PMCID: PMC3289637)
    16. A.M.L. Edström, V. Rydengard, P. Fernlund, M. Morgelin, M. Baungarten, A.M. Cole, M. Malmsten, B.B. Karglund, O.E. Sørensen. (2012). beta-microseminoprotein endows seminal plasma with potent calcium-dependent candidacidal activity at vaginal pH. PLoS Pathogens. 8(4): e1002625. (PMCID: PMC3320615)
    17. Gupta, P., D. Ratner, M. Ding, B. Patterson, L.C. Rohan, T. Reinhart, V. Ayyavoo, X. Huang, D.L. Patton, B. Ramratnam, and A.M. Cole. (2012). Retrocyclin RC-101 blocks HIV-1 transmission across cervical mucosa in an organ culture. J AIDS. 60(5):455-461. (PMCID: PMC3404240)
    18. Gupta, P., C. Lackman-Smith, D. Ratner, L.C. Rohan, D.L. Patton, B. Ramratnam, and A.M. Cole. (2012). Antiviral activity of retrocyclin RC-101, a candidate microbicide against cell-associated HIV-1. AIDS Res Hum Retroviruses. 29(2): 391-6. (PMCID: PMC3552163)
    19. Lamers, R.P., G. Muthukrishnan, T. A. Castoe, S. Tafur, A.M. Cole*, and C.L. Parkinson*. (2012). Phylogenetic relationships among Staphylococcus species and refinement of cluster groups based on multilocus data. BMC Evol Biol. 12: 171. (PMCID: PMC3464590) *Equal correspondence/authorship.  Designated “Highly accessed” article by BMC.
    20. Eade, C.R., C. Diaz, M.P. Wood, K. Anastos, B.K. Patterson, P. Gupta, A.L. Cole, and A.M. Cole. (2012). Identification and Characterization of Bacterial Vaginosis-Associated Pathogens Using a Comprehensive Cervical-Vaginal Epithelial Coculture Assay. PLoS ONE. 7(11): e50106. (PMCID: PMC3499514)
    21. Eade, C.R., A.L. Cole, C. Diaz, L.C. Rohan, M.A. Parniak, P. Marx, P.M. Tarwater, P. Gupta, and A.M. Cole. (2013). The Anti-HIV Microbicide Candidate RC-101 Inhibits Pathogenic Vaginal Bacteria Without Harming Endogenous Flora or Mucosa. Am J Reprod Immunol. 69(2):150-8. (PMCID: PMC3541468)
    22. Wood, M.P., A.L. Cole, P. Ruchala, A.J. Waring, L.C. Rohan, P. Marx, P.M. Tarwater, P. Gupta, and A.M. Cole. (2013). A Compensatory Mutation Provides Resistance to Disparate HIV Fusion Inhibitor Peptides and Enhances Membrane Fusion. PLoS ONE. 8(2):e55478.  (PMCID: PMC3564752)
    23. Muthukrishnan, G., R.P. Lamers, A. Ellis, V. Paramanandam, A.B. Persaud, S. Tafur, C.L. Parkinson, and A.M. Cole. (2013). Longitudinal genetic analyses of Staphylococcus aureus nasal carriage dynamics in a diverse population. BMC Infect Dis. 16(13): 221. (PMCID: PMC3673815)
    24. Wood, M.P., A.L. Cole, C.R. Eade, L.M. Chen, K.X. Chai, and A.M. Cole. (2014). The HIV-1 gp41 ectodomain is cleaved by matriptase to produce a chemotactic peptide that acts through FPR2. Immunology. (in press)

    Recent Reviews/Book Chapters

    1. Sivaraman, K., N. Venkataraman, and A.M. Cole. (2009). Staphylococcus aureus nasal carriage and its contributing factors. Future Microbiol. 4: 999-1008. (PMCID: PMC2908500).
    2. Penberthy, W.T., S. Chari, A.L. Cole, and A.M. Cole. (2011). Retrocyclins and their activity against HIV-1. in:  Host-defense peptides: from biology to therapeutic strategies. Editor:  M. Luisa Mangoni. Cell Mol Life Sci. 68(13): 2231-42.
    3. Eade, C.R., M.P. Wood, A.M. Cole. (2012). Mechanisms and modifications of naturally occurring host defense peptides for anti-HIV microbicide development. Curr HIV Res. 10(1): 61-72.
    4. Lehrer, R.I., A.M. Cole, and M.E. Selsted. (2012). Theta Defensins: cyclic peptides with endless potential. J Biol Chem. 287(32):27014-9. (PMCID: PMC3411038)

    For more publication information, please visit Pubmed.

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    Dr. Amy Cole
  • Title: Research Associate Professor
  • Office: BMS 236
  • Phone: 407.823.0918
  • Studies how bacterial vaginosis-associated bacteria alter mucosal barrier defense against HIV in the female reproductive tract (FRT), in the pursuit of new drugs that provide anti-HIV activity without disturbing the FRT mucosa and resident healthy microbiome.
  • Send an Email
  • Biography:

    Our research interests include the study of several factors that modulate inflammatory pathways in the female genital tract (FGT). We have identified cationic antimicrobial peptides that contribute to the anti-viral capabilities of vaginal fluid. Former student projects have also identified pro-HIV molecules produced by endocervical cells exposed to bacterial vaginosis-associated bacteria. Current studies include fractionation of these co-culture fluids in order to identify specific proteins effecting epithelial barrier function, NFkB activation, and chemotaxis of HIV target cells. We collaborate with faculty from UCF and abroad in the pursuit of therapeutics that provide potent anti-viral activity without disturbing the dynamic environment of the FGT mucosa. We are also a GCLP-certified specimen processing lab for the HIV Vaccine Trials Network, and perform clinical processing for several Orlando-area clinical trials.

    Representative Publications:

    1. Venkataraman, N., Cole, A.L.*, Svoboda, P., Pohl, J, Cole, A.M. Cationic polypeptides are required for anti-HIV-1 activity of human vaginal fluid. J. Immunol. 175(11): 7560-7, 2005
    2. Cole, A.L., Yang, O.O., Warren, A.D., Waring, A.J., Lehrer, R.I., Cole, A.M. HIV-1 adapts to a retrocyclin with cationic amino acid substitutions that reduce fusion efficiency of gp41. J. Immunol. 176(11): 6900-5, 2006
    3. Cole, A.L., Herasimtschuk, A., Gupta, P., Waring, A.J., Lehrer, R.I., and Cole, A.M. The retrocyclin analogue RC-101 prevents human immunodeficiency virus type 1 infection of a model human cervicovaginal tissue construct. Immunology 121(1): 140-5, 2007
    4. Keller M.J., Guzman, E., Hazrati, E., Kasowitz, A., Cheshenko, N., Wallenstein, S., Cole, A.L., Cole, A.M., Profy, A.T., Wira, C.R., Hogarty, K., Herold, B.C. PRO 2000 elicits a decline in genital tract immune mediators without compromising intrinsic antimicrobial activity. AIDS. 21(4): 467-476, 2007
    5. Fuhrman, C.A., Warren, A.D., Waring, A.J., Dutz, S.M., Sharma, S., Lehrer, R.I., Cole, A.L., and Cole, A.M. Retrocyclin (RC)-101 overcomes cationic mutations on the heptad repeat 2 region of HIV-1 gp41. FEBS J. 274(24): 6477-87, 2007
    6. Cole, A.M., Cole, A.L. Antimicrobial polypeptides are key anti-HIV-1 effector molecules of cervicovaginal host defense. Am. J. Reprod. Immunol. 59(1): 27-34, 2008
    7. Martellini, J.A., Cole, A.L., Venkataraman, N., Quinn, G.A., Svoboda, P., Gangrade, B.K., Pohl, J., Sorensen, O.E., Cole, A.M. Cationic polypeptides contribute to the anti-HIV-1 activity of human seminal plasma. FASEB J. 23(10): 3609-18, 2009
    8. Cole, A.M., Patton, D.L., Rohan, L.C., Cole, A.L., Cosgrove-Sweeney, Y., Rogers, N.A., Ratner, D., Sassi, A., Tarwater, P., Ramratnam, B., Ruchala, P., Lehrer, R.I., Waring, A.J., and Gupta, P.  The formulated microbicide RC-101 was safe and antivirally active following intravaginal application in pigtailed macaques.  PLoS ONE 5(11): e15111, 2010.
    9. Sassi, A.B., Cost, M.R., Cole, A.L., Cole, A.M., Patton, D.L., Gupta, P., and Rohan, L.C.   Formulation development of Retrocyclin-1 (RC-101) as an anti-HIV vaginal microbicide product.  Antimicrob Agents and Chemother 55(5): 2282-9, 2011
    10. Martellini, J.A., Cole, A.L., Svoboda, P., Stuchlik, O., Chen, L.M., Chai, K.X., Gangrade, B.K., Sorensen, O.E., Pohl, J., and Cole, A.M.  HIV-1 enhancing effect of prostatic acid phosphatase peptides is reduced in human seminal plasma.  PLoS ONE 6(1): e16285, 2011.
    11. Ruchala, P., Cho, S., Cole, A.L., Carpenter, C., Jung, C-L., Luong, H., Micewicz, E.D., Waring, A.J., Cole, A.M., Herold, B.C., Lehrer, R.I. Simplified theta-defensins: search for new antivirals. Int. J. Peptide Res. and Ther. Published online Sept 23, 2011
    12. Levinson, P., Choi, R.Y., Cole, A.L., Hirbod, T., Rhedin, S., Payne, B., Guthrie, B.L., Bosire, R., Cole, A.M., Farquhar, C., Broliden, K. HIV-Neutralizing Activity of Cationic Polypeptides in Cervicovaginal Secretions of Women in HIV-Serodiscordant Relationships. PLoS One 2012; 7(2):e31996. Epub 2012 Feb 28
    13. Eade, C.R., Diaz, C., Wood, M.P., Anastos, K., Patterson, B.K., Gupta, P., Cole, A.L., Cole, A.M. Identification and characterization of bacterial vaginosis-associated pathogens using a comprehensive cervical-vaginal epithelial coculture assay. PLOS One. 7(11): 250106 Epub 2012 Nov15
    14. Eade, C.R., Cole, A.L.*, Diaz, C., Rohan, L.C., Parniak, M.A., Marx, P., Tarwater, P.M., Gupta, P., Cole, A.M. The anti-HIV microbicide candidate RC-101 inhibits pathogenic vaginal bacteria without harming endogenous flora or mucosa. Amer J Rep Immunol. 69(2): 150-8, 2013
    15. Wood, M.P., Cole, A.L., Ruchala, P., Waring, A.J., Rohan, L.C., Marx, P., Tarwater, P.M., Gupta, P., Cole, A.M. A compensatory mutation provides resistance to disparate HIV fusion inhibitor peptides and enhances membrane fusion. PLOS One. 8(2):e55478 Epub 2013 Feb5
    16. Wood. M.P., Cole, A.L., Eade, C.R., Chen, LM, Chai, K.X., Cole, A.M. The HIV-1 gp41 ectodomain is cleaved by matriptase to produce a chemotactic peptide that acts through FPR2. Accepted to Immunology, March 6, 2014
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    Dr. Sean D. Moore
  • Title: Associate Professor
  • Office: BMS 336A
  • Phone: 407.823.2188
  • Focuses on bacterial physiology with an emphasis on how the quality of protein synthesis is affected by antibiotics and environmental factors.
  • Send an Email
  • Biography:

    My group uses the model organism E. coli to study basic cellular physiology with a focus on ribosome function. In all cells, these machines decode genetic material and make proteins in a process called translation. Because ribosomes are the target of many antibiotics, there has been extensive research into the mechanism ribosome function to understand how these drugs work and how microbes become resistant to them. However, there are several other highly conserved features of ribosomes (and factors associated with their assembly) that are important for protein synthesis, but the details of their activities have not been established and no drugs are known that influence their activities.

    Our goal is to establish the molecular mechanisms for several of these translation-related factors, including some proteins that are part of the ribosome and some that are implicated in helping the ribosomes get built. This information is important because it will allow researchers to explore new antibiotic targets and also to have a comprehensive model of protein synthesis in the study of disease.

    A typical strategy we employ is to use genetic systems to reveal the physiological pathways affected by translation factors, and then to interrogate those pathways using a combination of molecular biology, computational biology, and biochemistry. The lab has hosted several graduate students and many undergraduates for this research effort.

    In addition studies of protein synthesis, we also have an Applied Industrial Microbiology (AIM) program. AIM uses a collection of student-driven projects to combine classical microbiology with advanced molecular biology to put students in touch with industry before they graduate. Some examples include: identifying microbes responsible for food production and for detoxifying wastewater in bioreactors, identifying fungi that produce new medically important molecules, and studying the effects of microgravity on microbial physiology.

    For more information, please visit our lab web pages!

    Recent Publications

    1. S.D. Moore and K. Teter (2014) “Group-effort applied research: Expanding opportunities for undergraduate research through original, class-based research projects.” Biochem Mol Biol Educ. 2014 Jul 8;42(4):331-8. PMID: 24898007.
    2. A. Naganathan and S.D. Moore (2013) “Crippling the essential GTPase Der causes dependence on ribosomal protein L9.” J Bacteriol. 2013 Aug;195(16):3682-91. PMID: 23772068.
    3. A.C. Carr, K.L. Taylor, M.S. Osborne, B.T. Belous, J.P. Myerson, and S.D. Moore (2012) “Rapid depletion of target proteins allows identification of coincident physiological responses.” J Bacteriol. 2012 Nov;194(21):5932-40. PMID: 22942249.
    4. A.C. Carr and S. D. Moore (2012) “Robust quantification of polymerase chain reactions using global fitting.” PLoS One 7(5):e37640.  PMID: 22701526.

    For more publication information, please visit Pubmed.

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    Dr. Herve Roy
  • Title: Associate Professor
  • Office: Biomedical Research Annex (BRA) 128
  • Phone: 407.882.2253
  • Investigates lipid remodeling systems used by bacteria to adapt the biochemical properties of the plasma membrane to suit conditions in their environment.
  • Send an Email
  • Biography:
    The cellular envelope is the first layer of defense protecting the cell from the hostilities of the surrounding environment. In order to thrive in their ever-changing environmental conditions, bacteria have developed mechanisms to adapt the biochemical properties of their membranes in response to environmental cues. Aminoacyl-phosphatidylglycerol synthases (aaPGSs) are integral membrane proteins responsible for the biosynthesis of aminoacyl-phosphatidylglycerol (aa-PG) in the cytoplasmic membrane of various bacteria. These enzymes divert several aminoacyl-tRNAs (aa-tRNAs) from their normal use in protein biosynthesis and utilize the amino acids of these charged tRNAs for the modification of the polar head of the phosphatidylglycerol (PG) constituting the cytoplasmic membrane. Addition of amino acids to the glycerol moiety of PG decreases the net negative charge of the membrane, thereby lowering the cellular permeability to cationic molecules and altering the physiological properties of the bacterial envelope. In Staphylococcus aureus, lysylated PG confers resistance to cationic antibacterial agents such as the pore forming peptides produced by the innate immune response during host infection (e.g., defensins produced by human neutrophils), and provides resistance to several other cationic antimicrobials (i.e., aminoglycosides, betalactamines and glycopeptides). aa-PGs not only provide bacteria with resistance to cationic antimicrobial agents and host defenses during infection, but also to other environmental stressors such as those encountered during extreme osmotic or acidic conditions.
    Understanding the mechanisms of cell membrane permeation by antibiotics and the strategies utilized by bacteria to resist these antibiotics is crucial for the design of antimicrobial agents that target not only aaPGSs and their regulatory mechanisms, but also individual components of the remodeled membrane. The focus of our research is to define the structure-function relationship of aaPGS family members from a variety of microorganisms and to determine the extent of the different amino acids utilized by these enzymes for lipid modification. These studies will provide insight into the biological significance of aa-PGs and the role of these modified lipids in bacterial pathogenicity and environmental adaptation.
    Recent publications:
    1. Grube CD, Roy H. A Quantitative Spectrophotometric Assay to Monitor the tRNA-Dependent Pathway for Lipid Aminoacylation In Vitro. Journal of biomolecular screening. 2016; 21(7):722-8. PMID:27073192

    2. Smith AM, Harrison JS, Grube CD, Sheppe AE, Sahara N, Ishii R, Nureki O, Roy H. tRNA-dependent alanylation of diacylglycerol and phosphatidylglycerol in Corynebacterium glutamicum. Molecular microbiology. 2015; 98(4):681-93. NIHMSID: NIHMS733861 PMID:26235234  PMCID:PMC4639916

    3. Dare K, Shepherd J, Roy H, Seveau S, Ibba M. LysPGS formation in Listeria monocytogenes has broad roles in maintaining membrane integrity beyond antimicrobial peptide resistance. Virulence. 2014; 5(4):534-46. PMID:24603093  PMCID:PMC4063814

    4. Smith, A. M., Harrison, J. S., Sprague, K. M., and Roy, H. (2013)A conserved hydrolase responsible for the cleavage of aminoacylphosphatidylglycerol in the membrane of Enterococcus faecium. J. Biol. Chem. 288, 22768-22776

    5. Lorber B, Fischer F, Bailly M, Roy H, Kern D. Protein analysis by dynamic light scattering: methods and techniques for students. Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology. 2012; 40(6):372-82. PMID:23166025

    6. Zou SB, Hersch SJ, Roy H, Wiggers JB, Leung AS, Buranyi S, Xie JL, Dare K, Ibba M, and Navarre WW,  Loss of elongation factor P disrupts bacterial outer membrane integrity. J Bacteriol, 2012. 194(2): 413-425.
    7. Rogers TE, Ataide SF, Dare K, Katz A, Seveau S, Roy H, Ibba M. A pseudo-tRNA modulates antibiotic resistance in Bacillus cereus. PloS one. 2012; 7(7):e41248. PMID:22815980  PMCID:PMC3399842

    8. Zou SB, Roy H, Ibba M, and Navarre WW, Elongation factor P mediates a novel post-transcriptional regulatory pathway critical for bacterial virulence. Virulence, 2011. 2(2): 147-51.
    9. Roy H, Zou SB, Bullwinkle TJ, Wolfe BS, Gilreath MS, Forsyth CJ, Navarre WW, and Ibba M, The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-beta-lysine. Nat Chem Biol, 2011. 7(10): 667-9.
    10. Gilreath MS, Roy H, Bullwinkle TJ, Katz A, Navarre WW, and Ibba M, beta-Lysine discrimination by lysyl-tRNA synthetase. FEBS Lett, 2011. 585(20): 3284-8.
    11. Blaise M, Frechin M, Olieric V, Charron C, Sauter C, Lorber B, Roy H, and Kern D, Crystal Structure of the Archaeal Asparagine Synthetase: Interrelation with Aspartyl-tRNA and Asparaginyl-tRNA Synthetases. J Mol Biol, 2011. 412(3): 437-52.
    12. Banerjee R, Reynolds NM, Yadavalli SS, Rice C, Roy H, Banerjee P, Alexander RW, and Ibba M, Mitochondrial Aminoacyl-tRNA Synthetase Single-Nucleotide Polymorphisms That Lead to Defects in Refolding but Not Aminoacylation. J Mol Biol, 2011. 410(2): 280-93.
    13. Roy H and Ibba M, Bridging the gap between ribosomal and nonribosomal protein synthesis. Proc Natl Acad Sci U S A, 2010. 107(33): 14517-8.
    14. Reynolds NM, Ling J, Roy H, Banerjee R, Repasky SE, Hamel P, and Ibba M, Cell-specific differences in the requirements for translation quality control. Proc Natl Acad Sci U S A, 2010. 107(9): 4063-8.
    15. Navarre WW, Zou SB, Roy H, Xie JL, Savchenko A, Singer A, Edvokimova E, Prost LR, Kumar R, Ibba M, and Fang FC, PoxA, yjeK, and elongation factor P coordinately modulate virulence and drug resistance in Salmonella enterica. Mol Cell, 2010. 39(2): 209-21.
    16. Banerjee R, Chen S, Dare K, Gilreath M, Praetorius-Ibba M, Raina M, Reynolds NM, Rogers T, Roy H, Yadavalli SS, and Ibba M, tRNAs: cellular barcodes for amino acids. FEBS Lett, 2010. 584(2): 387-95.
    17. Zeng Y, Roy H, Preeti BP, Ibba M, and Chen S, Characterization of two seryl-tRNA synthetases in albomycin-producing Streptomyces sp. ATCC 700974. Antimicrob Agents Chemother, 2009. 53(11): 4619-27.
    18. Roy H and Ibba M, Broad range amino acid specificity of RNA-dependent lipid remodeling by multiple peptide resistance factors. J Biol Chem, 2009. 284(43): 29677-83.
    19. Roy H, Dare K, and Ibba M, Adaptation of the bacterial membrane to changing environments using aminoacylated phospholipids. Mol Microbiol, 2009. 71(3): 547-50.
    20. Roy H, Tuning the properties of the bacterial membrane with aminoacylated phosphatidylglycerol. IUBMB life, 2009. 61(10): 940-953.
    21. Ling J, So BR, Yadavalli SS, Roy H, Shoji S, Fredrick K, Musier-Forsyth K, and Ibba M, Resampling and editing of mischarged tRNA prior to translation elongation. Mol Cell, 2009. 33(5): 654-60.
    For more publication information, please visit Pubmed.
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    Dr. William T. Self
  • Title: Associate Director of Undergraduate Affairs & Associate Professor
  • Office: BMS 124
  • Phone: 407.823.4262
  • Studies the role of metalloenzymes in Clostridium difficile that play a primary role in energy metabolism, and in the role of selenoenzymes in a variety of bacterial model systems.
  • Send an Email
  • Biography:

    Our research focuses in two main areas: 1.) The study of the anti-inflammatory properties of cerium oxide-based materials and 2.) The study of the biology of selenium and the targeting of the metabolism of selenium in pathogens.

    Elucidating the anti-inflammatory properties of cerium oxide nanomaterials. Cerium oxide nanoparticles (nanoceria) have recently been shown to reduce oxidative and nitrosative stress in large number of studies using both cell culture and animal models. We have discovered that these nanoparticles can effectively act as superoxide dismutase and catalase mimetics. We have also observed nitric oxide radical scavenging and recently shown that these nanoparticles can accelerate the decay of the harmful oxidant peroxynitrite. In collaboration with Dr. Sudipta Seal, we are continuing to study the anti-inflammatory properties of this material and beginning to development various biomaterials using these interesting rare earth oxides.

    The uptake and metabolism of selenium. To date no specific transport proteins have been identified in any biological organism for the high-affinity transport of selenium. However it is known that selenium can be taken up with high affinity by mammalian cells and also by some bacteria, including E. coli. We continue to search for the molecular mechanism behind high affinity transport of selenium for the synthesis of selenoproteins in a variety of model systems.

    The role of selenoenzymes in pathogenic microbes. We are elucidating the role of Stickland reactions in the energy metabolism and toxin regulation of the nosocomial pathogen Clostridium difficile. Our underlying hypothesis: Growth of this and related anaerobes (C. botulinum, C. sporogenes, C. sticklandii, Treponema denticola) requires the presence of the selenium-dependent oxidoreductases glycine reductase and/or D-proline reductase for optimal growth.

    Recent Publications

    1. Janet M. Dowding, Wenjun Song, Kimberly Bossy, Ajay Karakoti, Amit Kumar, Andrew Kim, Blaise Bossy, Sudipta Seal, Mark Ellisman, Guy Perkins, William T. Self, Ella Bossy-Wetzel (2014) Cerium oxide nanoparticles protect against A-Beta induced mitochondrial fragmentation and neuronal cell death. Cell Death and Differentiation advance online publication 6 June 2014; doi: 10.1038/cdd.2014.72
    2. Dowding, J. M., Das, S., Kumar, A., Dosani, T., McCormack, R., Gupta, A., Sayle, T. X. T., Sayle, D. C., von Kalm, L., Seal, S. and W. T. Self (2013) Cellular Interaction and Toxicity Depends on Physiochemical Properties and Surface Modification of Redox Active Nanomaterial,  ACS Nano, 7 (6): 4855 -4868.
    3. Schanen, B. C., Das, S., Reilly, C., Warren, W. L., Self, W. T., Seal, S., and D. R. Drake III (2013) Immunomodulation and T helper TH1/TH2 response polarization by CeO2 and TiO2 nanoparticles. PLoS ONE 8(5): e62816.
    4. Dowding, J., Seal, S. and W. T. Self (2013) Cerium oxide nanoparticles accelerate the decay of peroxynitrite (ONOO-). Drug Deliv Transl Res. Volume 3, Issue 4, pp 375-379.
    5. Boullait, L., Self, W. T. and A. L. Sonenshein (2013) Proline-Dependent Regulation of Clostridium difficile Stickland Metabolism. J. Bacteriol. 195(4):844.
    6. Das, S., Singh, S., Singh, V., Joung, D., Dowding, J.M., Zhai, L., Khondaker, S.I., Self, W. T. and Sudipta Seal (2013) Oxygenated functional group density on graphene oxide: Its effect on cell toxicity. Part. Part. Syst. Charact. 30: 148 -157.
    7. Das, S, Dowding, J. M., Klump, K. E., McGinnis, J. F., Self, W. T. and S. Seal (2013) Cerium oxide nanoparticles: Applications and prospects in nanomedicine. Nanomedicine. 8(9):1483-508.
    8. W. T. Self and S. Rosario (2013) “Selenoenzymes and selenium trafficking: an emerging target for therapeutics”, in Metals in Cells, edited by Valeria Culotta and Robert S. Scott. Chichester, UK: John Wiley & Sons, Ltd, pp.421-428.
    9. Das, S., Singh, S., Dowding, J. M., Oommen, S., Kumar, A., Sayle, T.X.T., Saraf, S., Patra, C. R., Vlahakis, N. E., Sayle, D. C., Self, W. T. and S. Seal (2013) The induction of angiogenesis by cerium oxide nanoparticles through the modulation of oxygen in intracellular environments. Biomaterials 33(31): 7746-7755.
    10. Self, W. T. (2013) Selenium proteins containing selenocysteine. (book chapter) in Encyclopedia of Inorganic and Bioinorganic Chemistry. Robert A. Scott, Editor. John Wiley & Sons, Ltd, Chichester, United Kingdom.
    11. Dowding, J. M., Dosani, T., Kumar, A., Seal, S. and W. T. Self (2012) Cerium oxide nanoparticles scavenge nitric oxide radical (·NO). Chem. Comm. 48: 4896-4898.
    12. Singh, V., Das, S., Kumar, A., Singh, S., Self, W. T. and S. Seal (2012) A facile synthesis of PLGA encapsulated cerium oxide nano particles: Release kinetics and biological activity. Nanoscale. 4: 2597-2605.
    13. Srivastava, M., Singh, S. and W. T. Self (2011) Exposure to Silver Nanoparticles Inhibits Selenoprotein Synthesis and the Activity of Thioredoxin Reductase. Environ. Health Persp. 120:56-61.
    14. Singh, S., Dosani, T., Karakoti, A., Kumar, A., Seal, S. and W. T. Self (2011) A phosphate-dependent shift in redox state of cerium oxide nanoparticles and its effects on catalytic properties. Biomaterials 32:6745-6753.
    15. Srivastava, M., Mallard, C., Burke, T., Hancock, L. E. and W. T. Self (2011) A selenium-dependent xanthine dehydrogenase triggers biofilm proliferation in Enterococcus faecalis through oxidant production. J. Bacteriol. 193(7):1643-52.
    16. Cho J-H, Bass, M., Babu, S., Dowding, J. M., Self, W. T. and S. Seal (2011) Up conversion luminescence of Yb3+ -Er3+ codoped CeO2 nanocrystals with imaging applications. J. Luminescence 132(3):743-749.
    17. Hirst, S. M., Karakoti, A., Singh, S., Self, W. T, Seal, S., and C. M. Reilly (2011) Bio-distribution and In Vivo Antioxidant Effects of Cerium Oxide Nanoparticles in Mice. Environ. Toxicol. DOI: 10.1002/tox.20704
    18. Karakoti, A., Singh, S., Dowding, J. M., Seal, S. and William T. Self* (2010) Redox-active Radical Scavenging Nanomaterials. Chem. Soc. Rev. 39, 4422 -4432.
    19. Singh, S., Kumar, A., Karakoti, A., Seal, S. and W. T. Self (2010) Unveiling the mechanism of uptake and sub-cellular distribution of cerium oxide nanoparticles. Mol. Biosyst., 6, 1813-1820.
    20. Babu, S., Cho, J-H., Dowding, J., Heckert, E., Komanski, C., Soumen, D., Colon, J., Baker, C. H., Bass, M., Self, W. T. and S. Seal (2010) Multicolored redox active upconverter cerium oxide nanoparticle for bio-imaging and therapeutics. Chem. Comm., 46(37):6915-7.
    21. Pirmohamed, T., Dowding, J. M., Singh S., Wasserman, B., Heckert, E., Karakoti, A. S., King, J. E. S., Seal, S. and W. T. Self (2010) Nanoceria exhibit redox state-dependent catalase mimetic activity.  Chem. Comm., 46, 2736-2738.
    22. Vincent, A., Inerbaev, T., Babu, S., Karakoti, A., Self, W. T., Masunov, A., and Sudipta Seal (2010) Tuning Hydrated Nanoceria Surfaces: Experimental/Theoretical Investigations of Ion Exchange and Implications in Organic and Inorganic Interactions. Langmuir 26(10):7188-98.
    23. Wolfram M. Brück, W. M., Brück, T. B., Self, W. T., Reed, J. K., Nitecki, S. S. and Peter J. McCarthy (2010) Comparison of the anaerobic microbiota of deep water Geodia sp. and sandy sediments in the Florida straits The ISME Journal 4(5):686-99.
    24. Jackson-Rosario, S. and W. T. Self (2010) Targeting Selenium metabolism and selenoproteins: Novel avenues for drug discovery. Metallomics. 2:112-116.
    25. Self, W. T. (2010). “Selenium containing amino acids and selenoproteins”, In “Comprehensive Natural products Chemistry II Chemistry and Biology (CONAP II), Mander, L., Lui, H.-W., Eds.; Elsevier: Oxford, 2010, Volume 5, pp. 121-148.
    26. Karakoti, A., Singh, S., Kumar, A., Malinska, M., Kuchibhatla, S., Wozniak, K., Self, W., and S. Seal (2009) PEGylated Nanoceria as Radical Scavenger with Tunable Redox Chemistry. J. Amer. Chem. Soc. 131 (40): 14144 -14145.
    27. Schanen, B. C., Karakoti, A. S., Seal, S., Drake, D. R., Warren, W. L. and W. T. Self (2009) Exposure to Titanium Dioxide Nanomaterials Provokes Inflammation of an in Vitro Human Immune Construct. ACS Nano. 3 (9): 2523-2532.
    28. Jackson-Rosario, S. and W. T. Self (2009) Stannous salts inhibit selenium metabolism in the oral pathogen Treponema denticola. J. Bacteriol. 191(12): 4035-4040.
    29. Vincent, A., Babu, S, Heckert, E., Dowding, J., Hirst, S. M., Inerbaev, T. M., Self, W. T., Reilly, C. M., Masunov, A. M., and Sudipta Seal (2009) Protonated nanoparticle surface governing ligand tethering and cellular targeting. ACS Nano. 3 (5): 1203-1211.
    30. Jackson-Rosario, S., Cowart, D., Myers, A., Tarrien, R., Levine, R. L., Scott, R. and W. T. Self (2009). Auranofin disrupts selenium metabolism in Clostridium difficile by forming a stable Au-Se adduct: Identification and validation of a novel target for antimicrobial development. J. Biol. Inorg. Chem. May;14(4):507-19.
    31. Meno, S., Nelson, R., Hintze, K. J. and W. T. Self (2009). Exposure to monomethylarsonous acid (MMAIII) leads to altered selenoprotein synthesis in a primary human lung cell model.  Toxicol. Appl. Pharm. 239(2):130-136.

    For more publication information, please visit Pubmed.

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    Dr. Ken Teter
  • Title: Professor
  • Office: Biomedical Research Annex (BRA) 142
  • Phone: 407.882.2247
  • Studies the cell biology of AB-type protein toxins such as Shiga toxin, cholera toxin, and ricin.
  • Send an Email
  • Biography:

    My research program is focused on the cell biology of intoxication with AB-type protein toxins such as cholera toxin, Shiga toxin, and ricin.  These toxins are originally present in the extracellular milieu, but they attack targets within the cytosol of the host cell.  The toxins must therefore cross a membrane barrier in order to function.  A long-term goal of my laboratory is to elucidate the cellular events that allow toxin translocation, or entry, into the host cell cytosol.  If this process is understood at the molecular level, then rational therapies can be devised to block toxin translocation and, thus, productive intoxication.

    Recent publications

    1. Taylor M, Burress H, Banerjee T, Ray S, Curtis D, Tatulian SA, and Teter K.  2014.  Substrate-Induced Unfolding of Protein Disulfide Isomerase Displaces the Cholera Toxin A1 Subunit from Its Holotoxin.  PLoS Pathogens, 10(2):e1003925
    2. 

Teter K.  2013. Toxin Instability and Its Role in Toxin Translocation from the Endoplasmic Reticulum to the Cytosol.  (Review)  Biomolecules  3:997-1029.
    3. Reddy S, Taylor M, Zhao M, Cherubin P, Geden S, Ray S, Francis DH, and Teter K.  2013.  Grape Extracts Inhibit Multiple Events in the Cell Biology of Cholera Intoxication.  PLOS ONE  8(9):e73390
    4. Ray S, Taylor M, Banerjee T, Tatulian SA, and Teter K.  2012.  Lipid Rafts Alter the Stability and Activity of the Cholera Toxin A1 Subunit.  J Biol Chem  287(36):30395-30405
    5. Tapia-Pastrana G, Chavez-Dueñas L, Lanz-Mendoza H, Teter K, and Navarro-Garcia F.  2012.  VirK is a Periplasmic Protein Required for Efficient Secretion of Pet from Enteroaggregative E. coli.  Infect Immun  80(7):2276-2285
    6. 

Taylor M, Banerjee T, VanBennekom N, and Teter K.  2012.  Detection of Toxin Translocation into the Host Cytosol by Surface Plasmon Resonance.  J Vis Exp  59: pii: 3686. doi: 10.3791/3686.
    7. Massey S, Burress H, Taylor M, Nemec KN, Ray S, Haslam DB, and Teter K.  2011.  Structural and Functional Interactions Between the Cholera Toxin A1 Subunit and ERdj3/HEDJ, a Chaperone of the Endoplasmic Reticulum.  Infect Immun  79(11):4739-4747.
    8. Ray S, Taylor M, Burlingame M, Tatulian SA, and Teter K.  2011.  Modulation of Toxin Stability by 4-Phenylbutyric Acid and Negatively Charged Phospholipids.  PLoS ONE  6(8):e23692
    9. 

Massey S, Quiñones B, and Teter K.  2011.  A cell-based fluorescent assay to detect the activity of Shiga toxin and other toxins that inhibit protein synthesis. Methods Mol Biol  739:49-59.
    10. Taylor M, Banerjee T, Ray S, Tatulian SA, and Teter K.  2011.  Protein Disulfide Isomerase Displaces the Cholera Toxin A1 Subunit from the Holotoxin Without Unfolding the A1 Subunit.  J Biol Chem  286(25):22090-22100.
    11. Taylor M, Banerjee T, Navarro-Garcia F, Huerta J, Massey S, Burlingame M, Tatulian SA, and Teter K.  2011.  A Therapeutic Chemical Chaperone Inhibits Cholera Intoxication and Unfolding / Translocation of the Cholera Toxin A1 Subunit.  PLoS ONE  6(4):e18825.
    12. 

Kaittanis C, Banerjee T, Santra S, Santiesteban OJ, Teter K, and Perez JM.  2011.  Identification of Moecular-Mimicry-Based Ligands for Cholera Diagnostics using Magnetic Relaxation.  Bioconj Chem  22(2):307-314.
    13. Banerjee T, Pande A, Jobling MG, Taylor M, Massey S, Holmes RK, Tatulian SA, and Teter K.  2010.  Contribution of Subdomain Structure to the Thermal Stability of the Cholera Toxin A1 Subunit.  Biochemistry  49(41):8839-8846.
    14. Taylor M, Navarro-Garcia F, Huerta J, Burress H, Massey S, Ireton K, and Teter K.  2010.  Hsp90 is
Required for Transfer of the Cholera Toxin A1 Subunit from the Endoplasmic Reticulum to the Cytosol.  J Biol Chem  285(41):31261-31267.
    15. Navarro-Garcia F, Sonnested M, and Teter K.  2010.  Host-Toxin Interactions Involving EspC and Pet, Two Serine Protease Autotransporters of the Enterobacteriaceae.  (Review)  Toxins  2(5):1134-1147.
    16. Nemec, KN, Scaglione P, Navarro-García F, Huerta J, Tatulian SA, and Teter K.  2010.  A Host-Specific Factor is Necessary for Efficient Folding of the Autotransporter Plasmid-Encoded Toxin.  Biochimie  92(2):171-177.
    17. Massey S, Banerjee T, Pande AH, Taylor M, Tatulian SA, and Teter K.  2009.  Stabilization of the Tertiary Structure of the Cholera Toxin A1 Subunit Inhibits Toxin Dislocation and Cellular Intoxication.  J Mol Biol  393:1083-1096.
    18. Quinones B, Massey S, Friedman M, Swimley MS, and Teter K.  2009.  Novel Cell-Based Method to
Detect Shiga Toxin 2 from Escherichia coli O157:H7 and Inhibitors of Toxin Activity.  Appl Environ Microbiol  75(5):1410-1416.
    19. Guerra L, Nemec KN, Massey S, Tatulian SA, Thelestam M, Frisan T, and Teter K.   2009.  A Novel 
Mode of Translocation for Cytolethal Distending Toxin.  Biochim Biophys Acta  1793(3):489-495.

    Note: red indicates UCF graduate student; blue indicates UCF undergraduate; green indicates high school student

    Teaching Publications


    1. Moore SD and Teter K.  2014.  Group-Effort Applied Research (GEAR):  Expanding Opportunities for Undergraduate Research Through Original, Class-Based Research Projects.  Biochemistry and Molecular Biology Education.  42(4):331-338
    2. Borgon RA, Verity N, and Teter K.  2013.  PILOTing Undergraduate Students to Hands-On Teaching and Research Skills.  Journal of Microbiology & Biology Education.  14(1):35-46.
    3. 

Teter K and Engelking H.  2009.  A Career Opportunities in the Biomedical Sciences Seminar Series.  Focus on Microbiology Education  15(3):6-7.

     

     

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Dr. Robert Borgon                                                           Dr. Camilla Ambivero

Title: Assistant Professor                                                 Title: Assistant Professor

Office: HPA II 317                                                              Office: HPA II 309

Phone: 407.823.5798                                                        Phone: 407.823.0174

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Dr. Alicia Hawthorne

Title: Assistant Professor

Office: HPA II 338

Phone: 407.823.4866

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Affiliated Faculty

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Dr. Shibu Yooseph

Title: Professor of Computer Science,

Genomics & Bioinformatics Cluster Lead

Office: HEC 239A

Phone: 407-823-5307