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Mycoplasma fermentans

Muhlradt, P.F., Kiess, M., Meyer, H., Sussmuth, R., and Jung, G. (1997) Isolation, structure elucidation, and synthesis of a macrophage stimulatory lipopeptide from Mycoplasma fermentans acting at picomolar concentration../. Exp. Med. 185(11), 1951-1958. [Pg.260]

Brandenburg, K., Wagner, F., Muller, M., Heine, H., Andra, J., Koch, M.H.J., Zahringer, U., Seydel, U. Physicochemical characterization and biological activity of a glycoglycerolipid from Mycoplasma fermentans. Eur J Biochem 270 (2003) 3271-3279. [Pg.65]

Structures of (a) a novel glycolipid from Arthrobacter atrocyaneus, (b) 1,2-diacyl-cr-D-glucopyranosyl-sn-glycerol taurinamide from Hyphomonas jannaschina, and (c) a novel phosphochollne-contalning glycolipid from Mycoplasma fermentans. predominantly c/s-16 1a>7 and c/s-18 1a>7 R, predominantly n-16 0, n-18 0, and n-19 0... [Pg.1607]

Several studies have shown that PMN production of cytokines during microbial stimulation requires activation of MAPK. Using specific MAPK inhibitors, neutrophil IL-8 production in response to LPS, Mycoplasma fermentans membrane lipoproteins, type III group B streptococci, as well as TNF-a and GM-CSF was found to be dependent upon p38 MAPK [22-24,33]. The ERKl/2 and p38 MAPK are also involved in LPS andM. fermentans membrane lipoprotein-stimulated IL-8 production, as determined by inhibitor studies with PD98059 and SB203580 [22]. [Pg.99]

With this protocol the following templates were successfully sequenced Ure-aplasma urealyticwn, 0.75 Mb genome Mycoplasma fermentans, 1.2 Mb genome Streptococcus pneumoniae, 2.3 Mb genome Escherichia coli, 4.6 Mb genome. [Pg.192]

Franzoso G, Dimitrov DS, Blumenthal R, Barile MF, Rottem S. Fusion of Mycoplasma fermentans strain incognitas with T lymphocytes. FEBS Lett. 1992 303 251-4. [Pg.650]

Another specific application is the use of 0.1 pm syringe filters for the removal of mycoplasma in tissue culture work. They are capable of removing 99.99% of three common human mycoplasma species (M. hominis, M. salivarium and M. fermentans) and two common contaminants of fetal calf serum (M. arginini and Acholeplasma Laidlawii) [Hoffman, 1989]. [Pg.244]

Mycoplasma contamination is usually caused by any of five common species. The organisms and their natural hosts are M. hyorhinis (pig), M. arginini (cow), M. orale (man). A, laidlawii (cow), and M. fermentans (man). [Pg.33]

Each new batch of media ingredients should be subject to quality control before agar or broth preparation. It is especially important to show that new batches of pig and horse serum can support the growth of a representative sample of species found infecting cell cultures, e.g. any two of M. orale, M. hominis, M. fermentans, M. arginini, M, hyorhinis or A laidlawii. The National Collection of Type Cultures (Colindale, London, UK) or the American Type Culture Collection (Manassas, Virginia, USA) may supply type strains, or wild-type strains may be used. Stock positive control cultures may be kept frozen at -70°C in mycoplasma broth. [Pg.37]

Figure 1.7.1 Detection of mycoplasma by PCR in experimentally infected Vero cells. Amplifications performed with the primer set mollil + moUi2a (lane 1) Vero cells infected with M. arginini (lane 2) Vero cells infected with M. fermentans (lane 3) Vero cells infected with M. hyorhinis (lane 4) Vero cells infected with M. orale (lane 5) Vero cells infected with A. laidlawiv, (lane 11) moUicute-free Vero cells (lane 13) negative control (distilled water). Amplifications performed with the primer set mollil + molli2b (lane 6) Vero cells infected with A. laidlawii (lane 7) Vero cells infected with M. arginini, (lane 8) Vero cells infected with M. orale-, (lane 9) Vero cells infected with M. fermentans (lane 10) Vero cells infected with M. hyorhinis (lane 12) mollicute-free Vero cells (lane 14) negative control. Figure 1.7.1 Detection of mycoplasma by PCR in experimentally infected Vero cells. Amplifications performed with the primer set mollil + moUi2a (lane 1) Vero cells infected with M. arginini (lane 2) Vero cells infected with M. fermentans (lane 3) Vero cells infected with M. hyorhinis (lane 4) Vero cells infected with M. orale (lane 5) Vero cells infected with A. laidlawiv, (lane 11) moUicute-free Vero cells (lane 13) negative control (distilled water). Amplifications performed with the primer set mollil + molli2b (lane 6) Vero cells infected with A. laidlawii (lane 7) Vero cells infected with M. arginini, (lane 8) Vero cells infected with M. orale-, (lane 9) Vero cells infected with M. fermentans (lane 10) Vero cells infected with M. hyorhinis (lane 12) mollicute-free Vero cells (lane 14) negative control.
Mycoplasma cells may fuse with the cells of eukaryotic hosts M. fermentans fused CD4 Molt, and CD4 12E lymphocytes in vitro without visible cytotoxicity [69]. Mycoplasma contamination of human tumor cell cultures is frequent with mycoplasma cells attached to tumor cells [70a, b, 71]. However, M. fermentans, or M. penetrans in embryonic mouse cell cultures activated the rc-related vav proto-oncogene, and induced malignant transformation src, Rous sarcoma vav, sixth letter of the Hebrew alphabet standing for linkage or connection) [72] recently reviewed in [73]. [Pg.44]


See other pages where Mycoplasma fermentans is mentioned: [Pg.248]    [Pg.1607]    [Pg.1623]    [Pg.97]    [Pg.590]    [Pg.513]    [Pg.186]    [Pg.248]    [Pg.1607]    [Pg.1623]    [Pg.97]    [Pg.590]    [Pg.513]    [Pg.186]    [Pg.28]    [Pg.897]   
See also in sourсe #XX -- [ Pg.44 ]




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