ArticleCellular microbiology2015
The Streptococcus pyogenes NAD(+) glycohydrolase modulates epithelial cell PARylation and HMGB1 release.
Article in Cellular microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed, 30 citations in OpenAlex.
- Type III secretion system effector YfiD inhibits the activation of host poly(ADP-ribose) polymerase-1 to promote bacterial infection.Communications biology · 2024Article
- Roles of ADP-Ribosylation during Infection Establishment byPathogens (Basel, Switzerland) · 2023Review
- Structure of the Streptococcus pyogenes NADJournal of bacteriology · 2022Article
- Review
- TheJournal of bacteriology · 2021Article
- Pathogen induced subversion of NADCell death discovery · 2021Article
- PARP Inhibitors: An Innovative Approach to the Treatment of Inflammation and Metabolic Disorders in Sepsis.Journal of inflammation research · 2021Review
- Nicotinamide Increases Intracellular NADFrontiers in microbiology · 2020Article
- Review
- The Role of Streptococcal and Staphylococcal Exotoxins and Proteases in Human Necrotizing Soft Tissue Infections.Toxins · 2019Review
- Poly(ADP-Ribose) Polymerases in Host-Pathogen Interactions, Inflammation, and Immunity.Microbiology and molecular biology reviews : MMBR · 2019Review
- The Secreted Virulence Factor NADase of Group AFrontiers in immunology · 2019Article
- Group AFrontiers in cellular and infection microbiology · 2019Article
- NADCell reports · 2018Article
- NAD-Glycohydrolase Depletes Intracellular NADFrontiers in microbiology · 2018Article
- Binding of NADmBio · 2017Article
- Article
- Evolutionary Constraints Shaping Streptococcus pyogenes-Host Interactions.Trends in microbiology · 2017Review
- Applying Precision Medicine and Immunotherapy Advances from Oncology to Host-Directed Therapies for Infectious Diseases.Frontiers in immunology · 2017Article
- Exploring NAD+ metabolism in host-pathogen interactions.Cellular and molecular life sciences : CMLS · 2016Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Streptococcus pyogenes uses the cytolysin streptolysin O (SLO) to translocate an enzyme, the S. pyogenes NAD(+) glycohydrolase (SPN), into the host cell cytosol. However, the function of SPN in this compartment is not known. As a complication, many S. pyogenes strains express a SPN variant lacking NAD(+) glycohydrolase (NADase) activity. Here, we show that SPN modifies several SLO- and NAD(+) -dependent host cell responses in patterns that correlate with NADase activity. SLO pore formation results in hyperactivation of the cellular enzyme poly-ADP-ribose polymerase-1 (PARP-1) and production of polymers of poly-ADP-ribose (PAR). However, while SPN NADase activity moderates PARP-1 activation and blocks accumulation of PAR, these processes continued unabated in the presence of NADase-inactive SPN. Temporal analyses revealed that while PAR production is initially independent of NADase activity, PAR rapidly disappears in the presence of NADase-active SPN, host cell ATP is depleted and the pro-inflammatory mediator high-mobility group box-1 (HMGB1) protein is released from the nucleus by a PARP-1-dependent mechanism. In contrast, HMGB1 is not released in response to NADase-inactive SPN and instead the cells release elevated levels of interleukin-8 and tumour necrosis factor-α. Thus, SPN and SLO combine to induce cellular responses subsequently influenced by the presence or absence of NADase activity.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.