Gary L. Sloan

Professor Emeritus


Education

  • Ph.D., Microbiology, University of Oklahoma, 1972
  • Postdoctoral research: University of Texas at Austin

Research Interests

Production of extracellular enzymes by bacteria. Current research involves: studies on extracellular enzymes produced by staphylococci and streptococci that kill closely related organisms and the possible evolutionary relationships among some of these enzymes; studies on the cell wall modifications that allow these organisms to be resistant to their own bacteriolytic enzymes; and studies on the physiological significance of proteolytic processing of proenzyme forms of extracellular hydrolytic enzymes.

Selected Publications

Gargis, A.S., L.S. Heath, H.E. Heath, P.A. LeBlanc, S.R. Gargis, T.H. Harris, and G.L. Sloan.  2013.  Complete nucleotide sequences of plasmids pACK2 and pACK5 from Staphylococcus simulans biovar staphylolyticus. Plasmid 69:257 – 262.

Gargis, S.R., H.E. Heath, P.A. LeBlanc, L. Dekker, R.S. Simmonds, and G.L. Sloan. 2010. Inhibition of the activity of both domains of lysostaphin through peptidoglycan modification by the lysostaphin immunity protein. Appl. Environ. Microbiol. 76:6944 – 6946.

Gargis, A.S., A.H. Tate, L.S. Heath, H.E. Heath, P.A. LeBlanc and G.L. Sloan.  2010.  Complete nucleotide sequences of plasmids pACK1 and pACK3 from Staphylococcus simulans biovar staphylolyticus. Plasmid 64:104 – 109.

Gargis, S.R., A.S. Gargis, H.E. Heath, L.S. Heath, P.A. LeBlanc, M.M. Senn, B. Berger-Bächi, R.S. Simmonds, and G.L. Sloan. 2009. Zif, the zoocin A immunity factor, is a FemABX-like immunity protein with a novel mode of action. Appl. Environ. Microbiol. 75: 6205 – 6210.

Gargis, A.S., L.S. Heath, H.E. Heath, P.A. LeBlanc and G.L. Sloan. 2009. Characterization of pACK4, a mobilizable plasmid from Staphylococcus simulans biovar staphylolyticus. Plasmid 62:201 – 205.

Gargis, A.S., A.D. O’Rourke, G.L. Sloan, and R.S. Simmonds. 2009. Prevalence and acquisition of the genes for zoocin A and zoocin A resistance in Streptococcus equi subsp. zooepidemicus. J. Mol. Evol. 68:498 – 505.

Gargis, S.R., H.E. Heath, L.S. Heath, P.A. LeBlanc, R.S. Simmonds, B.D. Abbott, R. Timkovich, and G.L. Sloan. 2009. Use of 4-sulfophenyl isothiocyanate labeling and mass spectrometry to determine the site of action of the streptococcolytic peptidoglycan hydrolase zoocin A. Appl. Environ. Microbiol. 75:72 – 77.

Chen, Y., R.S. Simmonds, G.L. Sloan, and R. Timkovich. 2008. The metal binding site of zoocin A. J. Biol. Inorg. Chem. 13:855 – 860.

Akesson, M., M. Dufour, G.L. Sloan, and R.S. Simmonds. 2007. Targeting of streptococci by zoocin A. FEMS Microbiol. Lett. 270:155 – 161.

Heath, L. S., S. R. Gargis, S. R. Smithberg, H. P. Johnson, H. E. Heath, P. A. LeBlanc, and G. L. Sloan. 2005. Plasmid-specified FemABX-like immunity factor in Staphylococcus sciuri DD 4747. FEMS Microbiol. Lett. 249:227 – 231.

Heath, L.S., H.E. Heath, P.A. LeBlanc, S.R. Smithberg, M. Dufour, R.S. Simmonds, and G.L. Sloan. 2004. The streptococcolytic enzyme zoocin A is a penicillin-binding protein. 2004. FEMS Microbiol. Lett. 236:205 – 211.