Helicobacter pylori Adhesion to Carbohydrates

Aspholm, Marina; Kalia, Awdhesh; Rühl, Stefan; Schedin, Staffan; Arnqvist, Anna; Lindén, Sara K.; Sjöström, Rolf; Gerhard, Markus; Semino–Mora, Cristina; Dubois, A.; Unemo, Magnus; Danielsson, Dan; Teneberg, Susann; Lee, Woo Kon; Berg, Douglas E.; Borén, Thomas

doi:10.1016/s0076-6879(06)17020-2

Cited by 51 publications

(55 citation statements)

References 59 publications

(74 reference statements)

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“…Additional cultures were exposed to intact P. gingivalis at cell to bacteria ratios of 1:10 and 1:5 for 30 minutes and processed for total RNA or protein. In separate studies, P. gingivalis bacteria were washed in PBS, incubated in fluorescein isothiocyanate (100 g/ml for 30 minutes), 21 and washed in cell culture media before being added to macrophage monolayers for indicated times at room temperature. The cultures were examined for bacterial binding using a Zeiss fluorescence microscope (Carl Zeiss, Thornwood, NY).…”

Section: Myeloid Cell Preparation and Stimulationmentioning

confidence: 99%

Rapid Myeloid Cell Transcriptional and Proteomic Responses to Periodontopathogenic Porphyromonas gingivalis

Nares

Moutsopoulos

Angelov

et al. 2009

The American Journal of Pathology

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Long-lived monocytes, macrophages, and dendritic cells (DCs) are Toll-like receptor-expressing, antigenpresenting cells derived from a common myeloid lineage that play key roles in innate and adaptive immune responses. Based on immunohistochemical and molecular analyses of inflamed tissues from patients with chronic destructive periodontal disease, these cells, found in the inflammatory infiltrate, may drive the progressive periodontal pathogenesis. To investigate early transcriptional signatures and subsequent proteomic responses to the periodontal pathogen, Porphyromonas gingivalis, donor-matched human blood monocytes, differentiated DCs, and macrophages were exposed to P. gingivalis lipopolysaccharide (LPS) and gene expression levels were measured by oligonucleotide microarrays. In addition to striking differences in constitutive transcriptional profiles between these myeloid populations, we identify a P. gingivalis LPS-inducible convergent, transcriptional core response of more than 400 annotated genes/ESTs among these populations, reflected by a shared, but quantitatively distinct, proteomic response. Nonetheless, clear differences emerged between the monocytes, DCs, and macrophages. The finding that long-lived myeloid inflammatory cells, particularly DCs, rapidly and aggressively respond to P. gingivalis LPS by generating chemokines, proteases, and cytokines capable of driving T-helper cell lineage polarization without evidence of corresponding immunosuppressive pathways highlights their prominent role in host defense and progressive tissue pathogenesis. The shared, unique, and/or complementary transcriptional and proteomic profiles may frame the context of the host response to P. gingivalis, contributing to the destructive nature of periodontal inflammation.

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Section: Myeloid Cell Preparation and Stimulationmentioning

confidence: 99%

Rapid Myeloid Cell Transcriptional and Proteomic Responses to Periodontopathogenic Porphyromonas gingivalis

Nares

Moutsopoulos

Angelov

et al. 2009

The American Journal of Pathology

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“…The physiological significance of this interaction remains to be elucidated. SabA is also essential for binding of H. pylori to sialylated glycoconjugates on erythrocytes and neutrophils (5,7,8). The latter interaction leads to non-opsonic oxidative burst involving G protein signaling and activation of phosphatidylinositol 3-kinase (8).…”

mentioning

confidence: 99%

The Three-dimensional Structure of the Extracellular Adhesion Domain of the Sialic Acid-binding Adhesin SabA from Helicobacter pylori

Pang

Nguyen

Perry

et al. 2014

Journal of Biological Chemistry

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“…The abilities of H. pylori to adapt to various acidic environments and to adhere to the gastric epithelium play substantial roles in colonization and long-term persistence in the human stomach (7). Adherence prevents clearance of H. pylori during gastric mucous shedding and ensures that nutrients from damaged epithelial cells are consistently available to the bacterium (8).…”

mentioning

confidence: 99%

Repetitive Sequence Variations in the Promoter Region of the Adhesin-Encoding Gene sabA of Helicobacter pylori Affect Transcription

et al. 2014

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The pathogenesis of diseases elicited by the gastric pathogen Helicobacter pylori is partially determined by the effectiveness of adaptation to the variably acidic environment of the host stomach. Adaptation includes appropriate adherence to the gastric epithelium via outer membrane protein adhesins such as SabA. The expression of sabA is subject to regulation via phase variation in the promoter and coding regions as well as repression by the two-component system ArsRS. In this study, we investigated the role of a homopolymeric thymine [poly(T)] tract ؊50 to ؊33 relative to the sabA transcriptional start site in H. pylori strain J99. We quantified sabA expression in H. pylori J99 by quantitative reverse transcription-PCR (RT-PCR), demonstrating significant changes in sabA expression associated with experimental manipulations of poly(T) tract length. Mimicking the length increase of this tract by adding adenines instead of thymines had similar effects, while the addition of other nucleotides failed to affect sabA expression in the same manner. We hypothesize that modification of the poly(T) tract changes DNA topology, affecting regulatory protein interaction(s) or RNA polymerase binding efficiency. Additionally, we characterized the interaction between the sabA promoter region and ArsR, a response regulator affecting sabA expression. Using recombinant ArsR in electrophoretic mobility shift assays (EMSA), we localized binding to a sequence with partial dyad symmetry ؊20 and ؉38 relative to the sabA ؉1 site. The control of sabA expression by both ArsRS and phase variation at two distinct repeat regions suggests the control of sabA expression is both complex and vital to H. pylori infection.

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Helicobacter pylori Adhesion to Carbohydrates

Cited by 51 publications

References 59 publications

Rapid Myeloid Cell Transcriptional and Proteomic Responses to Periodontopathogenic Porphyromonas gingivalis

Rapid Myeloid Cell Transcriptional and Proteomic Responses to Periodontopathogenic Porphyromonas gingivalis

The Three-dimensional Structure of the Extracellular Adhesion Domain of the Sialic Acid-binding Adhesin SabA from Helicobacter pylori

Repetitive Sequence Variations in the Promoter Region of the Adhesin-Encoding Gene sabA of Helicobacter pylori Affect Transcription

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