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Titolo:
pH-regulated secretion of a glyceraldehyde-3-phosphate dehydrogenase from Streptococcus gordonii FSS2: Purification, characterization, and cloning ofthe gene encoding this enzyme
Autore:
Nelson, D; Goldstein, JM; Boatright, K; Harty, DWS; Cook, SL; Hickman, PJ; Potempa, J; Travis, J; Mayo, JA;
Indirizzi:
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA Univ Georgia Athens GA USA 30602 Biochem & Mol Biol, Athens, GA 30602 USA Inst Dent Res, Surry Hills, NSW, Australia Inst Dent Res Surry Hills NSW Australia Res, Surry Hills, NSW, Australia Louisiana State Univ, Hlth Sci Ctr, Dept Microbiol Immunol & Parasitol, New Orleans, LA USA Louisiana State Univ New Orleans LA USA & Parasitol, New Orleans, LA USA Jagiellonian Univ, Dept Microbiol & Immunol, Krakow, Poland Jagiellonian Univ Krakow Poland ept Microbiol & Immunol, Krakow, Poland
Titolo Testata:
JOURNAL OF DENTAL RESEARCH
fascicolo: 1, volume: 80, anno: 2001,
pagine: 371 - 377
SICI:
0022-0345(200101)80:1<371:PSOAGD>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
GROUP-A STREPTOCOCCI; ORAL STREPTOCOCCI; PLASMIN RECEPTOR; SURFACE PROTEIN; MUTANS; ENDOCARDITIS; EXPRESSION; SEQUENCE; GROWTH; IDENTIFICATION;
Keywords:
GAPDH; pH; Streptococcus gordonii;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
42
Recensione:
Indirizzi per estratti:
Indirizzo: Mayo, JA Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA Univ Georgia Athens GA USA 30602 Mol Biol, Athens, GA 30602 USA
Citazione:
D. Nelson et al., "pH-regulated secretion of a glyceraldehyde-3-phosphate dehydrogenase from Streptococcus gordonii FSS2: Purification, characterization, and cloning ofthe gene encoding this enzyme", J DENT RES, 80(1), 2001, pp. 371-377

Abstract

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 upregulated 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/09/20 alle ore 15:17:44