CCRC personnel

 

Carl Bergmann

Associate VP Research-Facilities; Associate Director, CCRC; Executive Director, Animal Health Research Center; Senior Research Scientist


Structure and function of the proteins that interact with anionic extracellular matrix polysaccharides in plants and animals

E-mail: cberg@ccrc.uga.edu
Telephone: 706-542-4487
Fax: 706-542-4412
Complex Carbohydrate Research Center
The University of Georgia
315 Riverbend Rd.
Athens, Georgia 30602

Short Biography
Research Interests
keywords and Selected Recent Publications
All Publications
Lab-personal web site

Short Biography:

Carl Bergmann received his Ph.D. in Organic Chemistry from the Ohio State University, and joined the Complex Carbohydrate Research Center as a postdoctoral research associate in 1986. He is currently a Senior Research Scientist. Dr. Bergmann’s research interests are in the biochemistry of acidic polysaccharides of plant and animal origin. Since 1990 he has served as the Facilities Director of the CCRC, which included the design and construction of two expansions of the original facility as well as overseeing the design and construction of the current CCRC facility. From 2007-2011, Dr. Bergmann served as Director of the Savannah River Ecology Laboratory in Aiken, South Carolina, and in 2008, he was appointed UGA Assistant Vice President for Research--Facilities. Full Publications: 41
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Research Interests:

The research pursued by my laboratory focuses on the structure and function of the proteins that interact with anionic extracellular matrix polysaccharides in plants and animals. Early research focused exclusively on proteins interacting with the (mammalian) glycosaminoglycans. In the last 15 years most of my work has centered on the degradation of pectins by fungal enzymes during pathogenesis and plant mechanisms to alter the rate at which that degradation occurs. The interaction of plant and fungal proteins during pathogenesis may have a profound effect on the success of the attempted fungal invasion, due in part to the structure of the cell wall oligosaccharides produced as a result of those interactions.

Investigating such interactions requires the ability to characterize both the proteins and the oligosaccharides produced. While much of this has been performed using traditional biochemical approaches, over the last several years my laboratory has moved toward a heavy involvement in mass spectrometry, done in collaboration with Ron Orlando and Lance Wells, and the use of surface plasmon resonance (SPR) spectrometry. Currently our work is focusing on combining biochemistry, SPR and mass spectrometry to investigate the mechanism of both hydrolysis and inhibition.

I am interested in applying this powerful set of tools to the study of mammalian matrix polysaccharides, as this work has served to highlight similarities between the mammalian and plant matrix polysaccharides and the enzymes that metabolize them. There is substantial evidence as to the roles of pectins in medicine including potentiation of human colonic adenocarcinoma cells, immunostimulating activity, anti- ulcer activity, anti-metastasis activity, anti-mutagenic activity, anti-nephrosis, and cholesterol decreasing activity. Our lab has been actively looking at the relationships between pectins and glycosaminoglycans, as well as between the microbial pectin degrading enzymes (PDEs) and microbial GAG degrading enzymes. It is a reasonable assumption that the receptors for GAGs involved in such activities as neural development and angiogenesis could act as potential targets for pectins and that the role of the GAGs themselves in neural development or angiogenesis may be altered by pectin degrading enzymes. Based on this hypothesis and our compelling in vitro data, we are currently investigating the in vivo role of pectins and PDE in modulating GAG function.
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Keywords and Selected Recent Publications:

Carbohydrate-protein interaction; glycosaminoglycans; mass spectrometry; surface plasmon resonance; glycosylation; endopolygalacturonase; polygalacturonase inhibiting proteins; pectin

Selected publications:

Stotz, H.U., J. Bishop, C.W. Bergmann, M. Koch, P. Albersheim, A.G. Darvill, and J.M. Labavitch. 2000. Identification of target amino acids that affect interactions of fungal polygalaturonases and their plant inhibitors. Physiol. Mol. Plant Pathol. 56: 117-130.

Kester, H.C.M., J.A.E. Benen, J. Visser, M.E. Warren, R. Orlando, C. Bergmann, D. Anker, and A. Doutheau. 2000. Tandem mass spectrometric analysis of Aspergillus niger pectin methylesterase; mode of action on fully methylesterified oligogalacturonides. Biochem. J. 346: 469-474.

Blumer, J.M., R.P. Clay, C.W. Bergmann, P. Albersheim, and A. Darvill. 2000. Temporal and spatial expression of pectin methylesterase in ripening tomato fruit and its correlation to the degree of pectin esterification in exopericarp cell walls. Can. J. Botany 78: 607-618.

Balandrán-Quintana, R.R., A.M. Mendoza-Wilson, C.W. Bergmann, I. Vargas-Arispuro, and M.A. Martínez-Téllez. 2002. Effect of pectic oligomers on physiological responses of chilling injury in discs excised from zucchini (Cucurbita pepo L.). Biochem. Biophys. Res. Comm. 290: 577-584.

Warren, M.E., H. Kester, J. Benen, J. Colangelo, J. Visser, C. Bergmann, and R. Orlando. 2002. Studies on the glycosylation of wild-type and mutant forms of Aspergillus niger pectin methylesterase. Carbohydr. Res. 337: 803-812.

King, D., M. Lumpkin, C. Bergmann, and R. Orlando. 2002. Studying protein-carbohydrate interactions by amide hydrogen/deuterium exchange mass spectrometry. Rapid Commun. Mass Spectrom. 16: 1569-1574.

King, D., C. Bergmann, R. Orlando, J.A.E. Benen, H.C.M. Kester, and J. Visser. 2002. The use of amide exchange-mass spectrometry to study conformational changes within the endopolygalacturonase II/homogalacturonans/polygalacturonase-inhibiting protein system. Biochemistry 41: 10225-10233.

Qin, Q., C.W. Bergmann, J.K.C. Rose, M. Saladie, V.S. Kumar Kolli, P. Albersheim, A.G. Darvill and W.S. York. 2003. Characterization of a tomato protein that inhibits a xyloglucan-specific endoglucanase. The Plant J. 34: 327-338.

Bergmann, C.W., L. Stanton, D. King, R.P. Clay, G. Kemp, R. Orlando, A. Darvill, and P. Albersheim. 2003. Recent observations on the specificity and structural conformation of the polygalacturonase-polygalacturonase inhibiting protein system. In: Pectins and Pectinases (F. Voragen, H. Schols, and R. Visser, eds.), pp. 277-291. Kluwer Academic Publishers, Dordrecht.

Kemp, G., C.W. Bergmann, R. Clay, A.J. Van der Wethuizen, and Z.A. Pretorius. 2003. Isolation of a polygalacturonase-inhibiting protein (PGIP) from wheat. Mol. Plant-Microbe Interact. 16: 955-961.

Kemp, G., Stanton, L., C.W. Bergmann, R.P. Clay, A. Darvill, and P. Albersheim. 2004. Polygalacturonase-inhibiting proteins can function as activators of polygalacturonse. Mol. Plant-Microbe Interact. 17: 888-894.

Xie, M., C. Bergmann, J. Benen, and R. Orlando. 2005. Post-translational modifications of recombinant B. cinerea EPG 6. Rapid Commun. Mass Spectrom. 19: 3389-3397.

Woosley, B., M. Xie, L. Wells, R. Orlando, D. Garrison, D. King, and C. Bergmann. 2006. Comprehensive glycan analysis of recombinant Aspergillus niger endopolygalacturonase C. Anal Biochem. In press.

Joubert, D.A., A.R. Slaughter, G. Kemp, C. Bergmann, G. Krooshoff, J. Benen, I.S. Pretorius, and M.A. Vivier. 2006. The grapevine polygalacturonase-inhibiting protein (VvPGIP1) reduces Botrytis cinerea susceptibility in transgenic tobacco and differentially inhibits fungal polygalacturonases. Transgenic Res. In press.
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