Molecular cloning and characterization of two
            <i>Helicobacter pylori</i>
            genes coding for plasminogen-binding proteins

Jönsson, Klas; Guo, Betty P.; Monstein, Hans‐Jürg; Mekalanos, John J.; Kronvall, Göran

doi:10.1073/pnas.0307329101

Cited by 47 publications

(33 citation statements)

References 32 publications

(30 reference statements)

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“…In an analysis of the detected peptides corresponding to this set of 39 proteins, 66% of the spectra were assigned to proteins previously annotated by Tomb et al (24) as outer membrane proteins (Fig. 2B), which is significantly higher than the corresponding values for any of the individual preparations (see (40), and several proteins identified annotated as "hypothetical proteins" (Table 2 and Fig. 2C).…”

Section: Resultsmentioning

confidence: 83%

Analysis of Surface-Exposed Outer Membrane Proteins in Helicobacter pylori

et al. 2014

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More than 50Helicobacter pylori genes are predicted to encode outer membrane proteins (OMPs), but there has been relatively little experimental investigation of the H. pylori cell surface proteome. In this study, we used selective biotinylation to label proteins localized to the surface of H. pylori, along with differential detergent extraction procedures to isolate proteins localized to the outer membrane. Proteins that met multiple criteria for surface-exposed outer membrane localization included known adhesins, as well as Cag proteins required for activity of the cag type IV secretion system, putative lipoproteins, and other proteins not previously recognized as cell surface components. We identified sites of nontryptic cleavage consistent with signal sequence cleavage, as well as C-terminal motifs that may be important for protein localization. A subset of surface-exposed proteins were highly susceptible to proteolysis when intact bacteria were treated with proteinase K. Most Hop and Hom OMPs were susceptible to proteolysis, whereas Hor and Hof proteins were relatively resistant. Most of the protease-susceptible OMPs contain a large protease-susceptible extracellular domain exported beyond the outer membrane and a protease-resistant domain at the C terminus with a predicted ␤-barrel structure. These features suggest that, similar to the secretion of the VacA passenger domain, the N-terminal domains of protease-susceptible OMPs are exported through an autotransporter pathway. Collectively, these results provide new insights into the repertoire of surface-exposed H. pylori proteins that may mediate bacterium-host interactions, as well as the cell surface topology of these proteins.

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Section: Resultsmentioning

confidence: 83%

Analysis of Surface-Exposed Outer Membrane Proteins in Helicobacter pylori

et al. 2014

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“…One mechanism by which H. pylori evades immune recognition may involve a form of antigenic disguise in which the bacteria are coated with host proteins. For example, H. pylori PgbA and PgbB proteins bind plasminogen, and the bacteria can thereby be coated with this host protein (108). Other mechanisms for evading immune recognition may involve phase variation and antigenic variation of surface components.…”

Section: Fig 2 Colonization Factors Of H Pylorimentioning

confidence: 99%

Helicobacter pyloriPersistence: an Overview of Interactions betweenH. pyloriand Host Immune Defenses

2006

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SUMMARY Helicobacter pylori is a gram-negative bacterium that persistently colonizes more than half of the global human population. In order to successfully colonize the human stomach, H. pylori must initially overcome multiple innate host defenses. Remarkably, H. pylori can persistently colonize the stomach for decades or an entire lifetime despite development of an acquired immune response. This review focuses on the immune response to H. pylori and the mechanisms by which H. pylori resists immune clearance. Three main sections of the review are devoted to (i) analysis of the immune response to H. pylori in humans, (ii) analysis of interactions of H. pylori with host immune defenses in animal models, and (iii) interactions of H. pylori with immune cells in vitro. The topics addressed in this review are important for understanding how H. pylori resists immune clearance and also are relevant for understanding the pathogenesis of diseases caused by H. pylori (peptic ulcer disease, gastric adenocarcinoma, and gastric lymphoma).

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“…The main phage-enabled technologies used to this end are phage display, bio-part development and genomic recombineering [156]. Phage display, a methodology involving fusing random peptide libraries to phage coat proteins, has yielded significant advances in the areas of vaccine development and drug delivery [156][157][158][159], with particular applications to management of Pseudomonas aeruginosa, Staphylococcus aureus and Bacillus anthracis [156]. Phage-based bio-part development represents a core strategy of synthetic biology.…”

Section: Synthetic Gene Network In Bacterial Antibiotic Resistance (mentioning

confidence: 99%

Mammalian synthetic biology: emerging medical applications

Kis

Pereira

Homma

et al. 2015

J. R. Soc. Interface.

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In this review, we discuss new emerging medical applications of the rapidly evolving field of mammalian synthetic biology. We start with simple mammalian synthetic biological components and move towards more complex and therapy-oriented gene circuits. A comprehensive list of ON-OFF switches, categorized into transcriptional, post-transcriptional, translational and posttranslational, is presented in the first sections. Subsequently, Boolean logic gates, synthetic mammalian oscillators and toggle switches will be described. Several synthetic gene networks are further reviewed in the medical applications section, including cancer therapy gene circuits, immuno-regulatory networks, among others. The final sections focus on the applicability of synthetic gene networks to drug discovery, drug delivery, receptor-activating gene circuits and mammalian biomanufacturing processes.

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Molecular cloning and characterization of two Helicobacter pylori genes coding for plasminogen-binding proteins

Cited by 47 publications

References 32 publications

Analysis of Surface-Exposed Outer Membrane Proteins in Helicobacter pylori

Analysis of Surface-Exposed Outer Membrane Proteins in Helicobacter pylori

Helicobacter pyloriPersistence: an Overview of Interactions betweenH. pyloriand Host Immune Defenses

Mammalian synthetic biology: emerging medical applications

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