Linda Chapman

Associate Professor of Biological Sciences

PhD, 1966 Univ. of California - Los Angeles

chapmanl@missouri.edu
573-882-1897
5 Tucker Hall

Research description

A recombinant n-acetyl galactosaminidase from Clostridium perfringens removes the terminal n-acetyl galactosamine (NAG) from the blood group A glycotopes on human red blood cell membranes; thereby converting cells of Blood Type A to cells of the universal donor, Blood Type O, at physiological pH. I have characterized functionally similar enzymes produced by marine bacteria. Although these enzymes have important applications in seroconversion, the function of the alpha galactosidases in bacterial physiology remains unknown.

I demonstrated the use of NAG as a carbon/energy source by Clostridium perfringens and marine bacteria of the genus Pseudoalteromonas.
I am investigating the pathway for the utilization of this amino sugar.

I am examining the role of NAG in the formation/structure of biofilms. Both Clostridia and Psedoalteromonas,like other microorganisms, form close associations with animal cells as a result of the formation of biofilms. Communication between the cells of the biofilm leads to the production of various metabolic products including the virulence factors which cause disease. Specifics of biofilm formation are important for understanding mechanisms of pathogenesis. My research has practical applications for drug development since antibiotics generally target metabolic pathways including those specific to the formation of surface macromolecules.

Selected publications

Hsieh, H.-Y., Calcutt, M.J., Chapman, L.F., Mitra, M., and Smith, D.S. 2005. Seroconversion of A2 to 0 red cell membranes with recombinant alpha-N-acetyl galactosidase. Artificial Cells, Blood Substitutes and Immobilization Biotechnology, 33: 187-1999.

Hsieh, H-Y, Calcutt, M.J., Chapman, L.F., Mitra, M., and Smith, D.S. 2003. Purification and characterization of recombinant alpha-N-acetylgalactosaminidase from Clostridium perfringens. Protein Expression and Purification 32: 309-316.

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