 | dgk501@med.unc.edu
630A Mary Ellen Jones
Campus Box 7290
Chapel Hill, NC 27599-7290
919.966.5307 |
Research
This laboratory has an ongoing interest in the structure and function of protein molecules. The bulk of our research concerns natural airborne allergens such as those from ragweed and grasses. Approaches to understanding and potentially manipulating the interaction of pollen allergens and the human immune system are multifaceted and include a broad range of technologies.
From a protein standpoint, the laboratory continues to isolate and characterize highly purified allergens. This characterization includes amino acid sequence analysis, chemical modification of allergens, and design of synthetic peptides which mimic human allergenic epitopes. Immunologic approaches in this system include making murine monoclonal antibodies to purified allergens, defining specific epitopes with those antibodies, and using selected monoclonal antibodies to inhibit the binding of human IgE antibodies to define allergenic epitopes in allergic individuals. Both B cell and T cell epitopes have been elucidated using various immunoassays. Among the molecular biological approaches utilized in the laboratory are the generation of genomic and cDNA libraries from pollen and other plant tissues, screening of those libraries for specific allergens, cloning and sequencing genes coding for allergens, and expression of engineered, recombinant allergens using various vectors.
Other approaches to understanding allergens and the immune response to them include use of combinatorial peptide libraries as the basis for novel vaccine design. In addition to our studies aimed at modulating the immune response to allergens, these combinatorial libraries have many other potential uses and form the basis of several scientific collaborations. We have also become involved in the design of liposome based delivery systems for peptides in an attempt to modify the immune response to selected antigens.
This laboratory has primary responsibility for the automated protein sequence and peptide synthesis facility which is housed in the Department. Instrumentation available in the facility includes, in addition to the protein sequencer and peptide synthesizers, a time-of-flight mass spectrometer, and several HPLC's which serve as ancillary equipment to support both the sequencer and synthesizers. We serve as a resource facility for the above technologies and a broad range of problems of biological interest come through the laboratory, allowing students an unusual opportunity to view and perhaps become involved in a breadth of scientific inquiry.
Cllick here to be taken to the Peptide Synthesis Facility.
Publications
Kuo, M.C., X.J. Zhu, R. Koury, I.J. Griffith, D.G. Klapper, J.F. Bond and B.L. Rogers. 1993. Purification and immunochemical characterization of recombinant and native ragweed allergen Amb a II. Mol. Immunology 12:1077-1087.
Ghosh, B., T. Rafnar, M.P. Perry, D. Bassolino-Klimas, W.J. Metzler, D.G. Klapper and D.G. Marsh. 1994. Immunologic and molecular characterization of Amb p V allergens from Ambrosia psilotachya (western ragweed) pollen. Journal of Immunology 152:2882.
Fulcher, K.D., J.E. Welch, D.G. Klapper, D.A. O'Brien and E.M. Eddy. 1995. Identification of a unique muclass glutathione S-transferase in mouse spermatogenic
cells. Mol. Reproduction & Dev. 42(4):415-424.
Hiller, K.M., R.E. Esch and D.G. Klapper. 1997. Mapping of an allergenically important determinant of grass group I allergens. Journal Allergy & Clinical Immunology 100:335-340.
Click here for a list of publications
Lab Page
http://microimm.med.unc.edu/pepsyn
Affiliations
