OSU Microbiology
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Well Known Schools that teaches Microbiology

Pharmaceutical and Generic Engineering firms are searching for Microbiologist. If you are in U.S and are in need of the best school that provides the best education for those who wanted to become a Microbiologist, the top 4 includes Harvard University, Stanford, University of California—​Berkeley, and University of Wisconsin—​Madison. These top 4 Universities are considered to be the best option to provide the best possible education for you.

Courses

The Difference Between Cell Biology and Microbiology

Cell Biology and Microbiology are almost simultaneous with each other every time we hear of these two disciplines. Somehow, there is a difference between the two as Cell Biology deals with the Cells in the human body, animals, plants and other living organisms while the Microbiology are for those that deals with microorganisms such as viruses and bacteria.

Privacy Policy

Privacy Policy Page

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OSUMICROBIOLOGY is committed to ensuring that your privacy is protected. Should we ask you to provide certain information by which you can be identified when using this website, then you can be assured that it will only be used in accordance with this privacy statement.

Osumicrobiology.org may change this policy from time to time by updating this page. You should check this page from time to time to ensure that you are happy with any changes. This policy is effective from December 2012.

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Graduate Programs

Ohio State Offers Training In Virtually Every Aspect Of Modern Microbiology

Ohio State Offers Training In Virtually Every Aspect Of Modern Microbiology

Our Ph.D. program in microbiology offers an individualized approach to graduate study in one of the nation’s largest teaching and research institutions. You will actively participate in planning your graduate program, working with colleagues from around the world while pursuing your Ph.D. degree.

Upon entering our graduate program, you will do five-week rotations in three laboratories of your choice. These rotations will expose you to a variety of researchers, their laboratories,Large fermentation unit and their specializations and should enable you to select an adviser who best suits your interests. Once you have selected your dissertation adviser — generally after about six months — you will work with your Ph.D. adviser to design a curriculum that complements your research project.

You will select courses from a broad spectrum of microbiology, including microbial genetics and physiology, immunology, fermentation technology, pathogenic microbiology, and environmental microbiology. You can also enroll in a variety of courses offered by related departments such as biochemistry, molecular genetics, and chemistry.

Your course work will be supplemented by participation in informal laboratory group meetings, journal clubs, and our departmental seminar series that features prominent research scientists at academic and industrial laboratories from Ohio State University and around the world. You will have the opportunity to meet with these scientists and discuss your research projects with them.

To help you develop communication skills, we offer a seminar series that gives you practice in presenting your work before a friendly audience. Each microbiology graduate student has several opportunities to present research papers at national or international meetings during his or her graduate career. Annual research competitions give you the opportunity to present your research to a wider audience and to compete for awards that honor the best presentations.

Graduate Programs

Graduate Admissions & Aid

Graduate Admissions & Aid

Please Note: It is now past the application deadline for Autumn 2009

If you have a bachelor’s or master’s degree in any of the biological sciences, biochemistry, molecular biology, genetics, engineering, or chemistry, you should apply directly to our Ph.D. program. The OSU Microbiology Graduate Program focuses on Ph.D. candidates, for whom full financial support is provided. Applicants to the M.S. program are less frequently admitted as financial aid cannot be guaranteed. In order to ensure full consideration, all applicants are strongly encouraged to have a completed application on file by December 31st. The university’s official application deadline for Autumn 2009 admission is January 15th. All supplemental application materials must be received by this date in order to participate in our regular on-campus interview process. You must submit results of the GRE general examination as part of your application. All international applicants whose native language is not English and who have not previously earned a U.S. degree must also pass the TOEFL examination. Visit the OSU Admissions Officeweb site for more information.

If you need additional information, call us at (614) 292-2301, send us a request by Fax at (614) 292-8120, or write:

Graduate Studies Chair
Department of Microbiology
The Ohio State University
484 West 12th Avenue
Columbus, OH 43210-1292

You may also request additional information by email from the Graduate Program Coordinator at micro.grad@osu.edu.

After we receive your completed application, we will make an admission decision and inform you of our decision in writing as soon as possible. Information about financial support will be included in the letter of admission.

In keeping with Ohio State’s commitment to affirmative action, the Department of Microbiology welcomes applications from members of underrepresented groups and encourages all applicants to visit our campus, tour our facilities, and meet with faculty and students in the program. Arrange to visit by calling our office.

We Guarantee Financial Aid

All qualified Ph.D. students are guaranteed financial support throughout their graduate program provided they remain in good academic standing and below 260 credit hours. We offer year-round support in the form of graduate associateships or fellowships. We also offer a variety of enrichment student fellowships. To apply for any of the fellowship opportunities, you must have a completed application on file by December 31st.

Graduate Teaching Associates (GTAs) spend no more than 20 hours each week teaching undergraduate and graduate courses in microbiology and biology. After one year as a Teaching Associate, there will be opportunities to become a Research Associate supported by a faculty member’s research grant while you complete your dissertation research.

Faculty Bios

Bacteriophage Ecology and Evolutionary Ecology

Stephen T. Abedon

Stephen T. Abedon

abedon.1@osu.edu

Associate Professor.
Ph.D., University of Arizona, 1990.

 

Bacteriophage Ecology and Evolutionary Ecology

Bacteriophage, or phage, are the viruses of bacteria. I am interested especially in phage adaptation: How phages can and have optimized their characteristics toward meeting the challenges of growth and survival. My research consists of a combination of theoretical and empirical analyses of phage population growth, and structure, as it occurs within both broth and semi-solid environments. My overall goal is to develop a more-complete theoretical understanding of the constraints acting on phage evolution.

Recent Publications

Calendar, R., Abedon, S.T. (eds) (in press). The Bacteriophages . Second Edition.

Abedon, S.T. (in press). Phage ecology. The Bacteriophages . Second Edition.

Abedon, S.T., Culler, R.R. (2007). Bacteriophage Evolution Given Spatial Constraint. Journal of Theoretical Biology, in press.

Abedon, S.T. (2006). Phage Ecology. In R. Calendar & S.T. Abedon (eds): The Bacteriophages Edition 2, Oxford University Press, pp. 37-46.

Abedon, S.T., LeJeune, J.T. (2005). Why Bacteriophage Encode Exotoxins and Other Virulence Factors. Evolutionary Bioinformatics Online 1:97-110.

Breitbart, M., Rohwer, F., Abedon, S.T. (2005). Phage Ecology and Bacterial Pathogenesis. In M.K. Waldor, D.I. Friedman, & S.L. Adhya (eds): Phages: Their Role in Bacterial Pathogenesis and Biotechnology, ASM Press, Washington, DC, pp. 66-91.

LeJeune J.T, Abedon, S.T., Takemura, K., Christie, N.P. and Sreevatsan, Human S. (2004). Escherichia coliO157:H7-Genetic marker in isolates of bovine origin. Emerging Infect. Dis. 10:1482-1485.

Goodridge, L., Abedon, S.T. (2003). Bacteriophage Biocontrol and Bioprocessing: Application of Phage Therapy to Industry. SIM News , 53:254-262. Click for PDF

Abedon, S.T. , Hyman, P., Thomas, C. (2003). Bacteriophage Latent-Period Evolution as a Response to Bacteria Availability: An Experimental Examination. Applied and Environmental Microbiology , 69:7499-7506. Click for PDF

Gill, J.J., Abedon, S.T. (2003). Bacteriophage Ecology and Plants. APSnet Feature , November 2003, http://www.apsnet.org/online/feature/phages/ . Click for PDF

Abedon, S.T. , Herschler, T. D., Stopar, D. (2001). Bacteriophage latent-period evolution as a response to resource availability. Applied and Environmental Microbiology 67:4233-4241. Click for PDF

Abedon, S.T. (2000). The murky origin of Snow White and her T-even Dwarfs. Genetics 155:481-486. Click for PDF

Abedon, S.T. (1999). Resistance to lysis-inhibition collapse. Genetical Research 74:1-11. Click for PDF

Paddison, P., Gailbreath, K., Dressman, H., Abedon, S.T. , Mosser, E., Neitzel, J., Guttman, B., Kutter, E. (1998) Lysis inhibition and fine-structure genetics in bacteriophage T4. Genetics. 148:1539-1550. Click for PDF

Abedon, S.T. (1994). Lysis and the interaction between free phages and infected cells. The Molecular Biology of Bacteriophage T4. Jim D. Karam, John W. Drake, Kenneth N. Kreuzer, Gisela Mosig, Dwight Hall, Frederick A. Eiserling, Lindsay W. Black, Elizabeth Kutter, Karin Carlson, Eric S. Miller, Eleanor Spicer (eds). Washington, DC ASM Press. pp. 397-405 Click for PDF

Abedon, S.T.(1992). Lysis of lysis-inhibited bacteriophage T4 infected cells. Journal of Bacteriology 174:8073-8080. Click for PDF

Abedon, S.T.(1990). Selection for lysis-inhibition in bacteriophage. Journal of Theoretical Biology 146:501-511. Click for PDF

Abedon, S.T. (1989). Selection for bacteriophage latent period length by bacterial density: A theoretical examination. Microbial Ecology 18:79-88. Click for PDF

Stephen T. Abedon Home Page , Phage Ecology , The Bacteriophages

Research Opportunities

Microbiology Faculty Interests

Active links indicate faculty members who are currently accepting
undergraduate researchers (Autumn 2003)

Name
Office (Phone#)
Email Research Interests Undergraduate projects
Stephen T. Abedon
Mansfield Campus (419-755-4343)
abedon.1@osu.edu Bacteriophage Evolutionary Ecology.
Brian M. Ahmer
934 Riffe Bldg
(292-1919)
ahmer.1@osu.edu Regulatory Networks in Pathogenic bacteria
Irina Artsimovitch
428 Biosci Bldg
(292-6777)
artsimovitch.1@osu.edu We study regulation of transcription in bacteria using primarily biochemical and molecular genetics approaches. We use RfaH, a bacterial protein required for pathogenesis, as a model system to dissect molecular mechanisms by which regulatory proteins affect activity of RNA polymerase. Specific projects suitable for undergraduate research include: (i) analysis of RfaH mutants; (ii) analysis of RfaH effect on gene expression using reporter constructs; (iii) identification of RfaH-responsive elements in bacterial genomes.
Neil R. Baker
541 Biosci Bldg
(292-3342)
baker.2@osu.edu Pathogenicity of Gram-Negative Pathogens
Paula Wolf Bryant
909 Biosci Bldg
(247-7694)
bryant.218@osu.edu The Role of MHC Class II-restricted Antigen Presentation in Pathogen and Tumor Immunity
Charles J. Daniels
428 Biosci Bldg
(292-6777)
daniels.7@osu.edu Molecular Biology of the Archaea: Transcription and Gene Regulation in the Archaea, RNA Processing and Genome Analysis
Kurt Fredrick

417 Biosci Bldg

(292-6679)

fredrick.5@osu.edu There are two independent projects in my lab: (1) understanding how the ribosome functions and (2) understanding how bacteria influence insect reproduction. Students have the opportunity to learn techniques in molecular biology, microbiology, biochemistry, and cell biology.
Tina M. Henkin
904 Riffe Bldg
(688-3831)
henkin.3@osu.edu My laboratory is interested in regulation of gene expression in bacteria at the level of premature termination of transcription, with Bacillus subtilis as our model system.
Michael Ibba
556 Biosci Bldg
(292-2120)
ibba.1@osu.edu Our lab works on protein synthesis in bacteria. We have openings for undergraduates interested in gaining experience in the areas of microbiology, molecular biology and biochemistry through participating in ongoing research projects.
Pravin T. Kaumaya
316 Medical Res.
Ctr (292-7028)
kaumaya.1@osu.edu Peptide and Protein Design, Antigenic and Immunogenic Determinants, Peptide and Protein Folding, Cancer Vaccines, Immunotherapy, Autoimmune Diseases, and Transplantation
Joseph A. Krzycki
914 Riffe Bldg.
(292-1578)
krzycki.1@osu.edu Our lab works on methanogens, members of the Archaea that make most of the world’s biologically produced methane. We recently discovered that these organisms possess a never before seen amino acid. This amino acid is encoded by amber codons in certain genes required to make methane. Amber codons are usually stop codons—but in these methanogens, they now act as sense codons. Undergraduates in our lab would work on some aspect of how this novel amino acid is made, and why the methanogens have changed their genetic code to include a new amino acid. They would also work on projects to uncover other organisms in nature that possess this novel amino acid.
Mark Morrison
Animal Science
230 Plumb Hall
(688-5399)
morrison.234@osu.edu Molecular Biology of Cellulose Degradation and Bacterial Adhesion to Surfaces One student is working on a proteomics-based analysis of bacterial responses to growth on cellulose and other polysaccharides. Another student is using Ribosomal Intergenic Spacer Analysis (RISA) to examine the microbial communtities present in the digestive tract of animals.
Richard F. Mortensen
555 Biosci Bldg
(292-3360)
mortensen.3@osu.edu We are investigating two related research projects that examine the cell-signalling pathways triggered by blood proteins that mediate innate or nonspecific host resistance. The projects look at both positive and negative (regulatory) signaling mechanisms in monocytes and neutrophils, using human cell lines. The technology used is cell culture, biochemistry, and immunochemistry.
Robert S. Munson
Pediatrics
Children’s Hospital
(722-2778)
munson.10@osu.edu
John N. Reeve
376 Biosci Bldg
(292-2301)
reeve.2@osu.edu We are investigating the molecular biology of microorganisms that live in boiling thermal vents and frozen in ice in glaciers. Specifically, we are determining how their proteins and DNA are stabilized and still function in such extreme environments
Abhay Satoskar
917 Biosci Bldg
(292-3243)
satoskar.2@osu.edu The leishmaniases comprise several diseases caused by intracellular protozoan parasites belonging to Leishmania species leading to a wide spectrum of clinical manifestations and a global health problem. Our laboratory is interested in understanding the immune mechanisms that determine outcome of “New world” cutaneous and visceral leishmaniasis caused by L. mexicana and L. donovani respectively.
F. Robert Tabita
700 Riffe Bldg
(292-4297)
tabita.1@osu.edu We are interested in the regulation of microbial carbon, nitrogen, and hydrogen metabolism. Students would be involved in projects that use molecular microbiology, biochemistry, genomics, and proteomics techniques.
Olli H. Tuovinen
622 Biosci Bldg
(292-3379)
olli.tuovinen@osu.edu Environmental and Industrial Microbiology
Marshall V. Williams
2074 Graves Hall
(292-0717)
williams.70@osu.edu Herpesviruses and Mutagenesis
Ahmed E. Yousef
217 Parker Hall
(292-7814)
yousef.1@osu.edu Food Microbiology, Microbial Safety of Food
Bruce S. Zwilling
612 Biosci Bldg
(292-3310)
zwilling.1@osu.edu Mycobacterial Resistance, Macrophage Activation, Regulation of Macrophage Gene expression by Corticosteroids and Neuroimmunology
Faculty Bios

Bacterial Pathogenesis and Genomics.

Robert S. Munson, Jr.

munson.10@osu.edu

Professor Department of Pediatrics

Bacterial Pathogenesis and Genomics.

Research Summary:
Nontypeable Haemophilus influenzae is an important cause of otitis media in children, and a major cause of lower respiratory disease in children in the developing world. The organism is also associated with exacerbations of chronic bronchitis, and pneumonia in elderly and immunocompromised patients.

Haemophilus ducreyi is the causative agent of chancroid, a sexually transmitted disease. Chancroid ulcers facilitate the transmission of HIV. My laboratory is employing a number of genetic and immunological approaches in order to assess the role of outer membrane proteins, toxins and adhesins in the pathogenesis of Haemophilus disease.

My laboratory is also interested in global regulation of expression of virulence determinants. We also have a major interest in bacterial genomics. Recently, we completed the sequence of the genome of H. ducreyi and we are currently annotating the sequence.

Recent Publications

Sun, S., Schilling, B., Tarantino, L., Tullius, M. V., Gibson, B. W. and Munson, R. S., Jr. (2000). Cloning and characterization of the lipooligosaccharide galactosyltransferase II gene of Haemophilus ducreyi. J Bacteriol 182 (8): 2292-8.

Young, R. S., Fortney, K., Haley, J. C., Hood, A. F., Campagnari, A. A., Wang, J., Bozue, J. A., Munson, R. S., Jr. and Spinola, S. M. (1999). Expression of sialylated or paragloboside-like lipooligosaccharides are not required for pustule formation by Haemophilus ducreyi in human volunteers. Infect Immun 67 (12): 6335-40.

Bozue, J. A., Tullius, M. V., Wang, J., Gibson, B. W. and Munson, R. S., Jr. (1999). Haemophilus ducreyi produces a novel sialyltransferase. Identification of the sialyltransferase gene and construction of mutants deficient in the production of the sialic acid-containing glycoform of the lipooligosaccharide. J Biol Chem 274 (7): 4106-14.

Cope, L. D., Lumbley, S., Latimer, J. L., Klesney-Tait, J., Stevens, M. K., Johnson, L. S., Purven, M., Munson, R. S., Jr., Lagergard, T., Radolf, J. D. and Hansen, E. J. (1997). A diffusible cytotoxin of Haemophilus ducreyi. Proc Natl Acad Sci U S A 94 (8): 4056-61.

Palmer, K. L. and Munson, R. S., Jr. (1995). Cloning and characterization of the genes encoding the hemolysin of Haemophilus ducreyi. Mol Microbiol 18 (5): 821-30

Faculty Bios

Peptide and Protein Design, Antigenic and Immunogenic Determinants, Peptide & Protein Folding

Pravin T. P. Kaumaya

Pravin T. P. Kaumaya

kaumaya.1@osu.edu

Professor
Ph.D., 1981, Portsmouth School of Pharmacy, England

Peptide and Protein Design, Antigenic and Immunogenic Determinants, Peptide & Protein Folding.

Research efforts in my laboratory are primarily based on exploiting the immune system’s exquisite specificity which offers one of the simplest and most effective ways to prevent and control disease. To achieve our goals a multidisciplinary research approach is being pursued which is at the interface of chemistry and biology with special emphasis on modulation of the immune response. We have and are continuing to develop innovative approaches to antigen specific vaccination as well as developing immunotherapies for cancer and autoimmune diseases. Therefore, we are actively pursuing an interdisciplinary approach to testing a novel multi-epitope cancer vaccine that bridges the synthetic, preclinical, and clinical elements of vaccine development. Several long term objectives include: 1) developing a widely applicable vaccine targeting the HER-2 oncoprotein (breast/ovarian/tumor/cancer vaccine and to gain understanding of immune response to self peptides in normal and pathologic conditions, 2) developing a widely applicable blockade strategy targeting costimulatory molecules (CD28:B7, CD40:CD40L) and also to elucidate the underlining mechanisms in downregulating immune responses as well as to gain understanding the biological active conformation of these peptide mimics and how they interact with the costimulatory molecules, 3) developing a B cell and T-cell vaccine for the retrovirus – HTLV-I (the causative agent of Adult T-cell Leukemia).

For peptide vaccines to become a practical reality, rationally designed, highly engineered synthetic constructs must incorporate enough antigenic determinants to elicit all three arms of the immune system. Novel vaccines designed to stimulate both antibody and T cell responses against human tumors are urgently required. It is critical to identify general rules for the definition of immunogenicity so that vaccine optimization is rational rather than empirical. Identification of the biologically relevant epitopes, devising strategies to engineer conformationally dependent sequences¸ adopting ways to increase the immunogenicity in an outbred population, delivering the immunogen in a safe and efficacious vehicle, developing animal models are at the basis of our approaches to developing new anticancer and retroviral vaccines. With these factors in mind, we have developed strategies for the design of PEPTIDE VACCINES that can provide optimal B cell, T helper cell and cytotoxic T cell responses. Our approach for the design of peptide vaccines with improved binding affinities, titers, and enhanced immunity a priori relies on the engineering of structured peptides which mimic antibody recognition sites and approaches to bypass MHC “restriction” of the T cell response. The immune responses (B-cell and T cell) to these peptides are then extensively studied to correlate biological or immunological reactivity with structure. This process of design, synthesis, structural characterization and immunological testing may point to a general strategy for tailoring peptide vaccines with more useful antigenic and immunogenic characteristics. Empirical and computational approaches are applied to the engineering and synthesis of complex peptide sequences designed to adopt well defined -secondary and three dimensional structures. A variety of biophysical techniques (CD, FTIR, SAXS, NMR, MS and X-Ray crystallography) are used to extensively characterize the chemical and structural properties of the synthetic peptides.

On the other spectrum of our research goals, overwhelming experimental evidence has emerged in recent years concerning the impact of costimulatory signals for complete T cell activation and has allowed investigators to develop new strategies for immune intervention, both for suppression of the immune system and for stimulation of the immune system. Attempts to block T cell costimulation as a therapeutic strategy in autoimmunity and transplantation have gained tremendous momentum. We are developing novel immunotherapeutic strategies that take advantage of normal mechanisms of tolerance to self antigen for immune intervention both for suppression of the immune system (autoimmune diseases (Multiple Sclerosis) and transplantation) and for stimulation of the immune system (vaccines). Our focus has been directed towards developing novel peptide mimics of ligand-binding regions of several costimulatory molecules (CD28:B7 and CD40:CD40L) in an attempt to block T cell costimulation pathways by use of retro-inverso (RI) modification of peptides that preserves the parent peptide overall topology and provides at the same time stability to proteolysis, leading to derivatives with prolonged half-life in vitro and in vivo. Blocking T cell costimulation as a therapeutic strategy in autoimmunity and transplantation is a major thrust in our laboratories.

Recent Publications

Kaumaya, P.T.P., Berndt, K., Heindorn, D., Trewhella, J., Kezdy, F.J. and Goldberg, E. (1990) Synthesis and Biophysical Characterization of Topographic Immunogenic Determinants with aa Topologies. Biochemistry, 29,13-23.

Kaumaya, P.T.P., VanBuskirk, A., Goldberg, E. and Pierce, S.K. (1992) Design and Immunological Properties of Topographic Immunogenic Determinants of a Protein Antigen (LDH-C4) as Vaccines. J. Biol. Chem., 267, 6338-6346.

Kaumaya, P.T.P., Seo, Y.H., Kobs, S., Ngua, l., Sheridan, J. and Stevens, V. (1993) Peptide vaccines incorporating a “promiscuous” T cell epitope bypass certain haplotype restricted immune responses and provide broad spectrum immunogenicity. J. Molec. Recog. 6, 81-94.

Kobs-Conrad, S., Lee, H., DiGeorge, A.M. and Kaumaya, P.T.P. (1993) Engineered Topographic Determinants with ab, bab, and baba Topologies show High Affinity Binding to Native Protein Antigen LDH-C4. J. Biol. Chem., 268, 25285-25295.

Lairmore, M.D., DiGeorge, A.M., Conrad, S.F., Trevino, A. and Kaumaya, P.T.P. (1995) HTLV-I Peptides Constructs incorporating Promiscuous T cell epitopes overcome genetic restriction, elicit neutralizing antibodies and T cell help. J. Virol.,69 (10),6077-6089

Kaumaya, P.T.P. (1996) Synthetic Peptide Vaccines: Dream or Reality. In Peptides in Immunology (Schneider, C.H., Ed.) Wiley and Sons, Ltd., pp. 117-148

Bakaletz, L. O., Leake, E. R., Billy, J. M., and Kaumaya, P. T. P. (1997) Relative Immunogenicity and Efficacy of Two Synthetic Chimeric Peptides of Fimbrin as Vaccinogens against Nasopharyngeal Colonization by Nontypeable Haemophilus Influenzae in the Chinchilla. Vaccine 15 (9), 955-961.

Dakappagari, N.K., Douglas, D.B., Triozzi, P.L., Stevens, V.C., and Kaumaya, P.T.P. (2000) Prevention of Mammary Tumors with a Chimeric HER-2 B-cell Epitope Peptide Vaccine. Cancer Research 60, 3782-3789

Frangione, M., Albretch, B., Dakappagari, N., Rose, T., Brooks, C.L., Schwendeman, S.P., Lairmore, M.D., and Kaumaya, P.T.P. (2001) Enhanced Immunogenicity of a Conformational Epitope of Human T-Lymphotropic Virus Type 1 using a Novel Chimeric Peptide. Vaccine 19, 1068-1081

Frangione-Beebe, M., Rose, T., Kaumaya, P.T.P., and Schwendeman, S.P. (2001) Microencapsulation of a Synthetic Peptide for HTLV-1 in Biodegradable Poly(D,L-lactise-co-glycolide) Microspheres using a Novel Encapsulation Technique. J. of Microencapsulation 18 (5), 663-677

Srinivasan, M., Wardrop, R.M., Whitacre, C., and Kaumaya, P.T.P. (2001) A Retro-Inverso Peptide Mimic of CD28 Encompassing the MYPPPY Motif Adopts a Polyproline Type II Helix and Inhibits Encaphalitogenic T cell in Vitro. J. Immunol 167:578-585

Roshni Sundaram, Christopher M Walker, and Pravin T.P. Kaumaya. (2001) Evaluation of HTLV-1 Cytotoxic T-cell Epitopes in HLA-A2.1 Transgenic Mice. In Peptides: The Wave of the Future (Eds Houghten R.A and Lebl, M) Kluwer Academic Publisher, Dordrecht, Netherlands. In Press

Pravin T.P. Kaumaya, John Pyles and Naveen Dakappagari. (2001) A combination of HER-2 peptide epitope vaccines mediate superior biological effects. In Peptides: The Wave of the Future (Eds Houghten R.A and Lebl, M) Kluwer Academic Publisher, Dordrecht, Netherlands. In Press

Sundaram, R., Dakappagari., and Pravin T.P. Kaumaya. (2002) Synthetic Peptides as Cancer Vaccine. Bioplolymers 66 (3),200-216

Sundaram, R, Yiping Sun, C.Walker, F.A.Lemonnier, S.Jacobson, and Pravin T.P. Kaumaya. (2003) A Novel HTLV-1 Epitope CTL Peptide Construct Elicits Robust Cellular Immune Responses in HLA-A*0201 Transgenic ß2 M, Db Double Knockout Mice. Vaccine 21, 2767-2781

Dakappagari, N., Parihar,R., J.Pyles, W.E. Carson, and Pravin T.P. Kaumaya. (2003) A Chimeric Multi HER-2 B cell epitope Peptide Vaccine mediates Superior Anti-tumor Responses. J. Immunol. 170:4242-4253

Utano Tomaru, Yoshihisa Yamano, Masahiro Nagai, Dragan Maric, Pravin T.P. Kaumaya, William Biddison, and Steven Jacobson. (2003) Acquisition of Peptide/HLA-GFP Complexes by Virus-Specific T Cells Differentiate Stages of T Cell Maturation Associated with The Outcome of Chronic Viral Infections. Nature Medicine 9(4), 469-475.

Sundaram, R., Beebe, M., and Kaumaya, P.T.P. (2004) Structural and Immunogenicity analysis of chimeric B-cell epitope constructs derived from gp46 and gp21 subunits of the env glycoproteins of HTLV-1. J. Peptide Res., 63, 132-140

Roshni Sundaram, Marcus P. Lynch , Sharad V. Rawale, Yiping Sun, Merdud Kazanji and Pravin T.P. Kaumaya. (2004) Denovo Design of Peptide Immunogens that Mimic the Coiled Coil Region of Human T-cell Leukemia Virus Type-1 gp21 Transmembrane Subunit for Induction of Native Protein Reactive Neutralizing Antibodies. J. Biol Chem., April 1, Epub ahead of Print); 279 (23) 24141-24151

Roshni Sundaram, Sharad Rawale , Naveen Dakappagari, Donn Young, Christopher M Walker, Francois Lemonnier, Steven Jacobson and Pravin T.P. Kaumaya. (2004) Protective Efiicacy of Multiepitope HLA-A*0201 restricted CTL Peptide construct against challenge with HTLV-1 TAX recombinant vaccinia virus. J. Acquir. Immune Defic. Syndr. 37 (3), 1329-1339

Roshni Sundaram, Melanie Beebe and Pravin T.P. Kaumaya (2004) Structural and Immunogenicity analysis of Chimeric B-cell epitope constructs derived from the gp46 and gp21 subunits of the env proteins of HTLV-1. J. Peptide Res. 63, 1-9

Naveen K. Dakappagari, Kenneth D. Lute, Sharad Rawale, Joan T. Steele, Stephanie D. Allen, Gary Phillips, R. Todd Reilly, and Pravin T.P. Kaumaya (2005) Conformational HER-2/neu B-Cell Epitope Peptide Vaccine Designed to Incorporate Two Native Disulfide Bonds Enhances Tumor Cell Binding and Antitumor Activities. J.Biol Chem (manuscript in press)

Faculty Bios

The Role of MHC-Restricted Antigen Presentation in the Immune Response Against Invading Microbial Pathogens and Tumors

Paula Wolf Bryant

bryant.218@osu.edu
Assistant Professor
Ph.D. – Baylor College of Medicine, 1988-1993
Postdoctoral fellowship – Harvard Medical School, 1993-2000

The role of MHC-restricted antigen presentation in the immune response against invading microbial pathogens and tumors.

The focus of research in my laboratory is the role of MHC-restricted antigen presentation in the immune response against invading microbial pathogens and tumors. To eliminate infected or transformed cells, the immune system must be capable of specifically recognizing antigen. Antigen-specific receptors on T lymphocytes recognize antigen only after it has been processed into small fragments or peptides, and presented on the cell surface bound in the peptide-binding cleft of major histocompatibility complex (MHC) class I and class II molecules. MHC class II molecules acquire peptide in the enodcytic pathway, and present their cargo to CD4+ T helper cells.

My research thus far has examined the machinery required to load class II molecules with antigenic peptides in healthycells of the mouse. Shortly after synthesis in the ER, MHC class II ab-dimers interact with a third glycoprotein, the invariant chain (Ii). Sorting signals in the cytoplasmic tail of Ii target class II molecules to their site of peptide binding in the endocytic pathway. As class II-Ii complexes traverse the endocytic route Ii is sequentially degraded by the combined action of cysteine- and aspartyl-proteases. Upon completion, a small fragment of Ii, CLIP, remains bound in the peptide-binding groove of class II. The final cleavage of Ii into CLIP is performed by the cysteine proteases Cathepsin S (Cat S) in B cells, dendritic cells macrophages, and Cathepsin L (Cat L) in Thymic Epithelial Cells. To complete peptide binding, most class II alleles require interaction with yet another accessory molecule, the nonclassical class II-dimer, DM. Interaction of DM with class II facilitates exchange of CLIP for antigenic peptides.

The requirements for DM and Cat S/L in class II peptide loading were defined by examining mice in which the genes encoding these accessory molecules were ‘knocked out’. These studies only examined antigen presentation in the uninfected host. Little is known about the role of class II-restricted antigen presentation in eliminating invading pathogens or tumors, and in resolution of disease, which is the current focus of my laboratory. Pathogens have developed means to escape immune recognition and destruction. How do microbes (i.e., mycobacterium) modify or abrogate the antigen presentation pathways of the host to avoid immune recognition and attack? Likewise, T cell tolerance is emerging as one of the leading mechanisms by which tumor cells evade immune recognition. Reactivity’s of CD4+ T cells that are restricted by MHC class II molecules have been documented against melanomas, lymphomas, colon cancers, and breast cancers. What is the antigen processing machinery used by tumor cells to process and present melanoma-associated antigens via class II molecules to CD4+ T cells? How does class II conformation influence acquisition and presentation bacterial-derived or tumor-derived antigens? What are the components of class II-restricted antigen presentation used by the host to elicit a T cell-mediated immune response against microbes, and against tumors? These questions are currently being addressed in my laboratory by using the various antigen presentation-deficient mice as infectious disease and tumor progression models.

Recent Publications

Wolf Bryant, P., Feibeger, E., Lennon-Duménil, A -M. Driessen, C., and H. L. Ploegh. (2001). Peptide loading of H-2-I-Ab molecules in the absence of Cat S is strictly DM-dependent. Submitted.

Lennon-Duménil, A -M., Bryant, R. A. R., Bikoff, E. R., Ploegh, H. L., and P. Wolf Bryant. (2001). The p41 Isoform of Invariant Chain is a Chaperone for Cathepsin L. EMBO J. in press.

Hsu, P. -N., Wolf Bryant, P., Sutkowski, N., McLellan, B., Ploegh, H. L., and B. T. Huber. (2001). Association of MMTV superantigen with MHC class II during biosynthesis. J. Immunol. 166: 3309-14.

Sant, A. J., Beeson, C., McFarland, H. F., Cao, B., Ceman, S., Bryant, P. W., and S. Wu. (1999). Individual hydrogen bonds play a critical role in MHC class II:peptide interactions: implications for the dynamic aspects of class II trafficking and DM-mediated peptide exchange. Immunol. Reviews. 172:239-53.

Wolf Bryant, P., Ceman, S., Sant, A. J., and H. L. Ploegh. (1999). Deviant trafficking of I-Ad mutant molecules is reflected in their peptide binding properties. Eur. J. Immunol. 9: 2729-39.

Driessen, C., Bryant, R. A. R., Lennon-Dumenil, A -M., Villadangos, J. A., Bryant, P. W., Shi, G. -P., Chapman, H. A., and H. L. Ploegh. (1999). Cathepsin S controls the trafficking and maturation of MHC class II molecules in dendritic cells. J. Cell Biol. 147:775-90.

Rodgers, J. R., Levitt, J., M., Cresswell, P., Lindahl, K. F., Mathis, D., Monaco, J. T., Singer, D. S., Ploegh, H. L., and P. Wolf Bryant. (1999). A nomenclature solution to mouse MHC confusion. J. Immunol. 162: 6294.

Wolf, P. R., Tourne, S., Miyazaki, T., Benoist, C., Mathis, D., and H. Ploegh. (1998). The phenotype of H-2M deficient mice is dependent on the class II molecules expressed. Eur. J. Immunol. 28: 2605-2618.

Wilson, N. A., Wolf, P., Ploegh, H., Ignatowicz, L., Kappler, J., and P. Marrack. (1998). Invariant chain can bind MHC class II at a site other than the peptide binding groove. J.Immuol. 161:4777-84.

Tourne, S., Miyazaki, T., Wolf, P., Ploegh, H., Benoist, C., and D. Mathis. (1997). Functionality of major histocompatibility complex class II molecules in mice doubly deficient for invariant chain and H-2M complexes. Proc. Natl. Acad. Sci. USA. 94: 9255-60.

Miyazaki, T., Wolf, P., Tourne, S., Waltzinger, C., Dierich, A., Barois, N., Ploegh, H., Benoist, C., and D. Mathis. (1996). Mice lacking H-2M complexes, enigmatic elements of the MHC class II peptide-loading pathway. Cell. 84: 531-41.

Riese, R. J., Wolf, P. R., Bromme, D., Natkin, L. R., Villadangos, J. A., Ploegh, H. L., and H. A. Chapman. (1996). Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading. Immunity. 4: 357-66.

Wolf, P. R., and H. L. Ploegh. (1995). How MHC class II molecules acquire peptide cargo: Biosynthesis and trafficking through the endocytic pathway. Annu. Rev. Cell Dev. Biol. 11: 267-306.

Wolf, P. R., and H. L. Ploegh. (1995). DM exchange mechanism. Nature. 376: 464-65.

Wolf, P. R., and R. G. Cook. (1995). The class I-b molecule Qa-1 forms heterodimers with H-2Ld and a novel 50-kD glycoprotein encoded centromeric to I-Eb. J. Exp. Med. 181: 657-68.

Wolf, P. R., and R. G. Cook. (1990). The TL region gene 37 encodes a Qa-1 antigen. J. Exp. Med. 172: 1795-1804.