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pH-regulated Secretion of a Glyceraldehyde-3-Phosphate Dehydrogenase from Streptococcus gordonii FSS2: Purification, Characterization, and Cloning of the Gene Encoding this Enzyme

Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602

J.M. Goldstein

Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602

K. Boatright

Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602

D.W.S. Harty

Institute of Dental Research, Surry Hills, New South Wales, Australia

S.L. Cook

Institute of Dental Research, Surry Hills, New South Wales, Australia

P.J. Hickman

Department of Microbiology, Immunology, and Parasitology, Louisiana State University Health Sciences Center, New Orleans, LA

J. Potempa

Department of Microbiology and Immunology, Jagiellonian University, Krakow, Poland

J. Travis

Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602

J.A. Mayo

Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, Department of Microbiology, Immunology, and Parasitology, Louisiana State University Health Sciences Center, New Orleans, LA

Streptococcus gordonii and other viridans streptococci (VS) are primary etiologic agents of infective endocarditis, despite being part of the normal oral microflora. Recently, a surface-bound glyceraldehyde-3 -phosphate dehydrogenase (GAPDH) has been found on the cells of all tested streptococcal species, where it has been implicated as a virulence factor. In contrast, we observed that a soluble extracellular GAPDH was the major secreted protein from S. gordonii FSS2, an endocarditis strain. The biochemical properties and gene sequence of S. gordonii GAPDH are almost identical to those of other streptococcal GAPDHs. Growth at defined pHs showed that secretion of GAPDH is regulated by environmental pH. GAPDH was primarily surface-associated at growth pH 6.5 and shifted to > 90% secreted at growth pH 7.5. Others have identified S. gordonii promoters that are up-regulated by a pH shift similar to that experienced by organisms entering the blood stream (neutral) from the oral cavity (slightly acid). Analysis of our results suggests that secretion of GAPDH may be a similar adaptation by S. gordonii.

Key Words: GAPDH • pH • Streptococcus gordonii

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Journal of Dental Research, Vol. 80, No. 1, 371-377 (2001)
DOI: 10.1177/00220345010800011301


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