J Biol Chem 1999, 274:37736–37742.PubMedCrossRef

37. Schraw W, Li Y, McClain MS, Goot FG, Cover TL: Association of Helicobacter pylori vacuolating toxin (VacA) with lipid rafts. J Biol Chem 2002, 277:34642–34650.PubMedCrossRef 38. Cao P, McClain MS, Forsyth MH, Cover TL: Extracellular release of antigenic proteins by Helicobacter pylori . Infect Immun 1998, 66:2984–2986.PubMed 39. Cover TL, Puryear W, Perez-Perez GI, Blaser MJ: Effect of urease on HeLa cell vacuolation induced by Helicobacter pylori HDAC inhibitor cytotoxin. Infect Immun 1991, 59:1264–1270.PubMed 40. Ilver D, Barone S, Mercati D, Lupetti P, Telford JL: Helicobacter pylori toxin VacA is transferred to host cells via a novel contact-dependent mechanism. Cell Microbiol 2004, 6:167–174.PubMedCrossRef 41. Ji X, Fernandez T, Burroni D, Pagliaccia C, Atherton JC, Reyrat JM, Rappuoli R, Telford JL: Cell specificity of

Helicobacter pylori cytotoxin is determined by a short region in the polymorphic midregion. Infect Immun 2000, 68:3754–3757.PubMedCrossRef 42. Pagliaccia C, de Bernard M, Lupetti P, Ji X, Burroni D, Cover TL, Papini E, Rappuoli R, Telford JL, Reyrat JM: The m2 form of the Helicobacter pylori cytotoxin has cell type-specific vacuolating GSI-IX activity. Proc Natl Acad Sci USA 1998, 95:10212–10217.PubMedCrossRef 43. Wang WC, Wang HJ, Kuo CH: Two distinctive cell binding patterns by vacuolating toxin fused with glutathione S-transferase: one high-affinity m1-specific selleck inhibitor binding and the other lower-affinity binding for variant m forms. Biochemistry 2001, 40:11887–11896.PubMedCrossRef 44. Oliver DC, Huang G, Nodel E, Pleasance S, Fernandez RC: A conserved region within the Bordetella pertussis autotransporter BrkA is necessary for folding of its passenger domain. Mol Microbiol 2003, 47:1367–1383.PubMedCrossRef 45. Junker M, Besingi

RN, Clark PL: Vectorial transport and folding of an autotransporter virulence protein during outer membrane secretion. Mol Microbiol 2009, 71:1323–1332.PubMedCrossRef Authors’ contributions Conceived and designed the experiments: SEI, MSM, DBL, TLC. Performed the experiments: SEI. Analyzed the data: SEI, MSM, HMSA, DBL, TLC. Wrote the paper: SEI, TLC. All authors read and approved the final manuscript.”
“Background S. mutans is considered the major etiological agent of dental 3-oxoacyl-(acyl-carrier-protein) reductase caries due to its strong aciduric and acidogenic capacities. During the metabolism of dietary carbohydrates and subsequent formation of acid end-products, acidogenic bacteria can shift the plaque pH to 4 or lower within minutes and can retain it at this value for up to one hour, depending on the age of the plaque biofilm [1–4]. Demineralisation of the tooth enamel caused by low pH is the beginning of caries development. To withstand these pH fluctuations and to compete with other oral bacteria S. mutans has evolved an effective acid tolerance response (ATR).