ABSTRACT
No disponible
Subject(s)
Humans , Male , Female , Meningitis/complications , Meningitis/diagnosis , /complications , Pneumococcal Infections/complications , Pneumococcal Infections/diagnosis , Mycoplasma salivarium/pathogenicity , Arthroscopy , Early Diagnosis , Ambulatory Surgical Procedures/methods , Ambulatory Surgical Procedures/trends , Viridans Streptococci/pathogenicityABSTRACT
We aimed to determine whether mycoplasmas are present in Korean chronic gastritis, and to understand their roles in gastric cancer tumorigenesis, because mycoplasmas resemble Helicobacter pylori in terms of ammonia production and induction of inflammatory cytokines in immune and non-immune cells. The presence and identity of mycoplasmas were assessed by semi-nested PCR and sequencing, and the results were compared with pathologic data. Fifty-six samples collected from Korean chronic gastritis patients were used for this study. Twenty-three (41.1%) were positive for mycoplasmas. Eighteen sequenced samples contained a single human mycoplasma or two mycoplasmas, which were identified as Mycoplasma faucium (13/18), M. fermentans (3/18), M. orale (1/18), M. salivarium (2/18), and M. spermatophilum (1/18). Mycoplasma-infected chronic gastritis samples showed significantly more severe neutrophil infiltration than non-infected samples (P = 0.0135). Mycoplasma profiles in the oral cavity (M. salivarium is major) and stomach were different, and the presence of significant proinflammatory responses in mycoplasma-positive patients suggests that the mycoplasmas are not simply contaminants. Further studies are required to understand whether mycoplasmas play a role in gastric tumorigenesis.
Subject(s)
DNA, Bacterial/isolation & purification , Gastritis/microbiology , Mycoplasma Infections/microbiology , Mycoplasma/isolation & purification , Stomach Neoplasms/etiology , Chronic Disease , Gastritis/metabolism , Gastroscopy , Humans , Korea/epidemiology , Molecular Sequence Data , Mouth/microbiology , Mycoplasma/genetics , Mycoplasma/pathogenicity , Mycoplasma Infections/epidemiology , Mycoplasma Infections/genetics , Mycoplasma fermentans/genetics , Mycoplasma fermentans/isolation & purification , Mycoplasma fermentans/pathogenicity , Mycoplasma salivarium/genetics , Mycoplasma salivarium/isolation & purification , Mycoplasma salivarium/pathogenicity , Organ Specificity , Pyloric Antrum/microbiology , Sequence Analysis, DNA , Stomach/microbiologyABSTRACT
The lipopeptide FSL-1 [S-(2,3-bispalmitoyloxypropyl)-Cys-Gly-Asp-Pro-Lys-His-Pro-Lys-Ser-Phe, Pam(2)CGDPKHPKSF] synthesized on the basis of the N-terminal structure of a Mycoplasma salivarium lipoprotein capable of activating normal human gingival fibroblasts to induce the cell surface expression of ICAM-1 revealed an activity to induce production of monocyte chemoattractant protein 1, interleukin-6 (IL-6), and IL-8. FSL-1 also activated macrophages to produce tumor necrosis factor alpha as the Mycoplasma fermentans-derived lipopeptide MALP-2 (Pam(2)CGNNDESNISFKEK), a potent macrophage-activating lipopeptide, did. The level of the activity of FSL-1 was higher than that of MALP-2. This result suggests that the difference in the amino acid sequence of the peptide portion affects the activity because the framework structure other than the amino acid sequence of the former is the same as that of the latter. To determine minimal structural requirements for the activity of FSL-1, the diacylglyceryl Cys and the peptide portions were examined for this activity. Both portions did not reveal the activity. A single amino acid substitution from Phe to Arg and a fatty acid substitution from palmitic acid to stearic acid drastically reduced the activity. Similar results were obtained in measuring the NF-kappaB reporter activity of FSL-1 to human embryonic kidney 293 cells transfected with Toll-like receptor 2 and 6, together with a NF-kappaB-dependent luciferase reporter plasmid. These results suggest that both the diacylglyceryl and the peptide portions of FSL-1 are indispensable for the expression of biological activities and for the recognition by Toll-like receptors 2 and 6 and that the recognition of FSL-1 by Toll-like receptors 2 and 6 appears to be hydrophobic.
