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Faculty Detail    
Name DAVID G PRITCHARD
 
Campus Address KAUL 502 Zip 0024
Phone  (20-5) -753
E-mail  davidp1@uab.edu
Other websites
     


Faculty Appointment(s)
Appointment Type Department Division Rank
Primary  Biochemistry & Molecular Genetics  Biochemistry & Molecular Genetics Professor Emeritus

Graduate Biomedical Sciences Affiliations
Biochemistry and Molecular Genetics Program 
Cellular and Molecular Biology Program 
Medical Scientist Training Program 
Microbiology 

Biographical Sketch 
David G. Pritchard (b. 1945), Professor of Biochemistry and Molecular Genetics, received his Ph.D. degree in biochemistry from the University of California at Los Angeles in 1975. He then spent 3 years at the City of Hope Research Institute in Duarte, California, studying the human tumor marker carcinoembryonic antigen. After coming to Birmingham in 1977, Dr. Pritchard began studying the protein and polysaccharide antigens of group B streptococci and their roles in pathogenesis. He has recently become interested in characterizing the glycoproteins on the surface of B. anthracis spores.



Research/Clinical Interest
Title
Roles of Bacterial Glycoconjugates in Pathogenesis
Description
My research interests are focused primarily on several different microbial products that contribute to the virulence of gram-positive bacteria, with particular emphasis on group B streptococcus (GBS) and Bacillus anthracis. GBS are a major cause of life-threatening infections of newborn babies in this country. In one project we are biochemically characterizing a hyaluronan lyase secreted by GBS and studying its role in pathogenesis. In another project we are genetically engineering a commensal organism normally present in the vagina of women, a lactobacillus, to secrete a bacteriophage lysin that will prevent vaginal colonization with group B streptococci (GBS), and thereby greatly reduce the incidence of serious neonatal GBS infections. Bacillus anthracis, the causative agent of anthrax, has already been used in bioterrorist attacks in this country and the potential for future large-scale attacks remains a serious concern. One means by which B. anthracis bacteria protect themselves from lysozyme present in blood and other bodily fluids is by deacetylating their peptidoglycan coat. We are attempting to identify the deacetylases involved in this process, with the long-term goal of developing drugs that inhibit the enzymes. This should make the bacteria susceptible to lysozyme in the blood and may provide an alternative therapeutic strategy. In another anthrax-related project we are characterizing a rhamnose-containing glycoprotein, BclA, on the surface of anthrax spores. Mutant spores that are unable to make rhamnose are much less virulent in a mouse model of anthrax.

Selected Publications 
Publication PUBMEDID
Baker, J.R., Yu, H., Morrison, K., Averett, W.F., and Pritchard, D.G. Specificity of the Hyaluronate Lyase of Group B Streptococcus toward Unsulfated Regions of Chondroitin Sulfate. Biochem. J. 327: 65-71 (1997).  9355736 
Lin, B., Averett, W.F., and Pritchard, D.G. Identification of a Histidine Residue Essential for Enzymatic Activity of Group B Streptococcal Hyaluronate Lyase. Biochem. Biophys. Res. Commun. 231: 379-382 (1997)  9070283 
Lin, B., Averett, W.F., Novák, J., Chatham, W.W., Hollingshead, S.K., Coligan, J.E., Egan, M.L., and Pritchard, D.G. Characterization of PepB, a Group B Streptococcal Oligopeptidase. Infect. Immun. 64: 3401-3406 (1996).  8757883 
Pritchard, D.G., and Lin, B. Group B Streptococcal Neuraminidase is Actually a Hyaluronidase. Infect. Immun. 61: 3234-3239 (1993).  8335355 
Pritchard, D.G., Lin, B., Willingham, T.R., and Baker, J.R. Characterization of the Group B Streptococcal Hyaluronate Lyase. Arch. Biochem. Biophys. 315: 431-437 (1994).  7986088 
Lin, B., Hollingshead, S.K., Coligan, J.E., Egan, M.L., Baker, J.R., and Pritchard, D.G. Cloning and Expression of the Gene for Group B Streptococcal Hyaluronate Lyase. J. Biol. Chem. 269: 30113-30116 (1994).  7982914 
Pritchard, D.G., Gray, B.M., and Egan, M.L. Murine Monoclonal Antibodies to the Type Ib Polysaccharide of Group B Streptococci Bind to Human Milk Oligosaccharides. Infect. Immun. 60: 1598-1602 (1992).  1548081 
Pritchard, D. G., Dong, S., Baker, J. R., and Engler, J. A. The Bifunctional Peptidoglycan Lysin of Streptococcus agalactiae Bacteriophage B30. Microbiology 150: 2079-2087 (2004).   15256551 
Daubenspeck, J. M., Zeng, H., Chen, P., Dong, S., Steichen, C. T., Krishna, N. R., Pritchard, D. G., and Turnbough, Jr., C. L. Novel Oligosaccharide Side-Chains of the Collagen-Like Region of BclA, the Major Glycoprotein of the Bacillus anthracis Exosporium. J. Biol. Chem. 279: 30945-30953 (2004)   15152001 
Baker J. R., Dong, S., and Pritchard, D. G. The Hyaluronan Lyase of Streptococcus pyogenes Bacteriophage H44890. Biochem. J. 365: 317-322 (2002).  12071858 
Baker J. R. and Pritchard, D. G. Action Pattern and Substrate Specificity of the Hyaluronate Lyase from Group B Streptococci. Biochem. J. 348: 465-471(2000).  10816443 
Pritchard, D. G., J. Trent, X. Li, P. Zhang, and J. R. Baker. Characterization of the Active Site of Group B Streptococcal Hyaluronan Lyase. Proteins 40: 126-134 (2000).  10813837