| 1. |
- Odenbreit, Stefan, et al.
(author)
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Outer membrane protein expression profile in Helicobacter pylori clinical isolates
- 2009
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In: Infection and Immunity. - 0019-9567 .- 1098-5522. ; 77:9, s. 3782-3790
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Journal article (peer-reviewed)abstract
- The gram-negative gastric pathogen Helicobacter pylori is equipped with an extraordinarily large set of outer membrane proteins (OMPs), whose role in the infection process is not well understood. The Hop (Helicobacter outer membrane porins) and Hor (Hop-related proteins) groups constitute a large paralogous family consisting of 33 members. The OMPs AlpA, AlpB, BabA, SabA, and HopZ have been identified as adhesins or adherence-associated proteins. To better understand the relevance of these and other OMPs during infection, we analyzed the expression of eight different omp genes (alpA, alpB, babA, babB, babC, sabA, hopM, and oipA) in a set of 200 patient isolates, mostly from symptomatic children or young adults. Virtually all clinical isolates produced the AlpA and AlpB proteins, supporting their essential function. All other OMPs were produced at extremely variable rates, ranging from 35% to 73%, indicating a function in close adaptation to the individual host or gastric niche. In 11% of the isolates, BabA was produced, and SabA was produced in 5% of the isolates, but the strains failed to bind their cognate substrates. Interleukin-8 (IL-8) expression in gastric cells was strictly dependent on the presence of the cag pathogenicity island, whereas the presence of OipA clearly enhanced IL-8 production. The presence of the translocated effector protein CagA correlated well with BabA and OipA production. In conclusion, we found unexpectedly diverse omp expression profiles in individual H. pylori strains and hypothesize that this reflects the selective pressure for adhesion, which may differ across different hosts as well as within an individual over time.
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| 2. |
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| 3. |
- Walz, Anke, et al.
(author)
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Identification of glycoprotein receptors within the human salivary proteome for the lectin-like BabA and SabA adhesins of Helicobacter pylori by fluorescence-based 2-D bacterial overlay
- 2009
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In: Proteomics. - : Wiley. - 1615-9853 .- 1615-9861. ; 9:6, s. 1582-1592
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Journal article (peer-reviewed)abstract
- Because gastric infection by Helicobacter pylori takes place via the oral route, possible interactions of this bacterium with human salivary proteins could occur. By using modified 1- and 2-D bacterial overlay, binding of H. pylori adhesins BabA and SabA to the whole range of salivary proteins was explored. Bound salivary receptor molecules were identified by MALDI-MS and by comparison to previously established proteome maps of whole and glandular salivas. By use of adhesin-deficient mutants, binding of H. pylori to MUC7 and gp-340 could be linked to the SabA and BabA adhesins, respectively, whereas binding to MUC5B was associated with both adhesins. Binding of H. pylori to the proline-rich glycoprotein was newly detected and assigned to BabA adhesin whereas the SabA adhesin was found to mediate binding to newly detected receptor molecules, including carbonic anhydrase VI, secretory component, heavy chain of secretory IgA1, parotid secretory protein and zinc-alpha(2)-glycoprotein. Some of these salivary glycoproteins are known to act as scavenger molecules or are involved in innate immunity whereas others might come to modify the pathogenetic properties of this organism. In general, this 2-D bacterial overlay technique represents a useful supplement in adhesion studies of bacteria with complex protein mixtures.
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| 4. |
- Aspholm, Marina, et al.
(author)
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Helicobacter pylori adhesion to carbohydrates
- 2006
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In: Methods in Enzymology. - 0076-6879 .- 1557-7988. ; 417, s. 293-339
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Journal article (peer-reviewed)abstract
- Adherence of bacterial pathogens to host tissues contributes to colonization and virulence and typically involves specific interactions between bacterial proteins called adhesins and cognate oligosaccharide (glycan) or protein motifs in the host that are used as receptors. A given pathogen may have multiple adhesins, each specific for a different set of receptors and, potentially, with different roles in infection and disease. This chapter provides strategies for identifying and analyzing host glycan receptors and the bacterial adhesins that exploit them as receptors, with particular reference to adherence of the gastric pathogen Helicobacter pylori.
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| 5. |
- Liu, Qingcao, et al.
(author)
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Ionization-Induced Subcycle Metallization of Nanoparticles in Few-Cycle Pulses
- 2020
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In: ACS Photonics. - : American Chemical Society (ACS). - 2330-4022. ; 7:11, s. 3207-3215
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Journal article (peer-reviewed)abstract
- Strong-field laser-matter interactions in nanoscale targets offer unique avenues for the generation and detailed characterization of matter under extreme conditions. Field-driven, subcycle ionization-induced metallization of nanoscale solids in intense laser fields has been predicted (Peltz et al. Time-Resolved X-ray Imaging of Anisotropic Nanoplasma Expansion. Phys. Rev. Lett. 2014, 113, 133401), but its observation was hampered by a lack of a smoking gun. Here, we report the ultrafast metallization of isolated dielectric and semiconducting nanoparticles under intense few-cycle laser pulses. The highest-energy electron emission is found to be a decisive proof that shows a characteristic cutoff modification to a metallic limit for intensities high enough to ignite carrier avalanching in the volume of the particles. Semiclassical Mean-field Mie Monte-Carlo transport simulations reveal the underlying dynamics and explain the observed evolution by near-field driven electron backscattering from the metallizing target.
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