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Human serum antibody response against iron-repressible outer membrane proteins of Helicobacter pylori (1996)

Worst, Dennis J. ; Sparrius, Marion ; Kuipers, Ernst J. ; [et al.]

Oxford, UK : Blackwell Publishing Ltd

FEMS microbiology letters 144 (1996), S. 0

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ISSN: 1574-6968

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Biology

Notes: Abstract In Helicobacter pylori, in vitro iron limitation induces the expression of several iron repressible outer membrane proteins (IROMPs), which are not expressed under normal growth conditions. To substantiate their proposed role in virulence of H. pylori, we determined whether these IROMPs are also expressed in vivo. Therefore, we tested whether sera of patients with H. pylori infection contained antibodies against IROMPs. All sera from 20 H. pylori positive patients showed a clear immune response against a 77 kDa heme-binding IROMP in an immunoblot assay. Antibody responses against the other IROMPs were also found, but with lower frequencies. Serum samples from 18 patients negative for H. pylori infection did not show any immunoreactivity with IROMPs. These results indicate that the IROMPs of H. pylori are immunogenic and are expressed in vivo.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1574-6968.1996.tb08504.x

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Effectors of the mammalian plasma membrane NADH-oxidoreductase system. Short-chain ubiquinone analogues as potent stimulators (1996)

Vaillant, FranÇois ; Larm, Jari A. ; McMullen, Gabrielle L. ; [et al.]

Springer

Journal of bioenergetics and biomembranes 28 (1996), S. 531-540

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ISSN: 1573-6881

Keywords: Plasma membrane NADH-oxidoreductase ; NADH-oxidase ; NADH∶ferricyanide reductase ; ubiquinone analogues ; ρ0 cells

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Chemistry and Pharmacology , Physics

Notes: Abstract In the presence of effectors variations in the two recognized activities of the plasma membrane NADH-oxidoreductase system were studied in separate, specificin vitro assays. We report here that ubiquinone analogues that contain a short, less hydrophobic side chain than coenzyme Q-10 dramatically stimulate the NADH-oxidase activity of isolated rat liver plasma membranes whereas they show no effect on the reductase activity of isolated membranes. If measured in assays of the NADH∶ferricyanide reductase of living cultured cells these compounds have only a limited effect; the oxidase activity of whole cells is not measurable in our hands. We have furthermore identified selective inhibitors of both enzyme activities. In particular, the NADH-oxidase activity can be significantly inhibited by structural analogues of ubiquinone, such as capsaicin and resiniferatoxin. The NADH∶ferricyanide reductase, on the other hand, is particularly sensitive to pCMBS, indicating the presence of a sulfhydryl group or groups at its active site. The identification of these specific effectors of the different enzyme activities of the PMOR yields further insights into the function of this system.