Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The ClpXP Protease Contributes to Staphylococcus aureus Pneumonia.

The Journal of infectious diseases - 14 Sept 2020

Kim Gyu-Lee, Akoolo Lavoisier, Parker Dane

Abstract excerpt

Staphylococcus aureus is a leading cause of pneumonia. We show here that the ClpXP protease involved in protein turnover is important for pathogenesis in a murine model of acute pneumonia. Staphylococcus aureus lacking this protease is attenuated in vivo, being rapidly cleared from the airway and leading to decreased immune cell influx and inflammation. Characterization of defined mutations in vitro identified...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Disease Models, Animal
Share to Endopeptidase Clp
Share to Host-Pathogen Interactions

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Inflammation

Share to Mice, Inbred C57BL

Share to Microbial Viability

Share to Neutrophils

Share to Staphylococcus aureus

Source

Open in PubMed Open full text

Identifiers

PMID: 32386322
DOI: 10.1093/infdis/jiaa251
PMCID: PMC7488198

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The ClpXP Protease Contributes to Staphylococcus aureus Pneumonia.PMID 32386322Read ↗

The ClpXP protease is dispensable for degradation of unfolded proteins in Staphylococcus aureusSemantic proximity Read ↗

Staphylococcus aureus ClpX localizes at the division septum and impacts transcription of genes involved in cell division, T7-secretion, and SaPI5-excisionSemantic proximity Read ↗

Trapping and Proteomic Identification of Cellular Substrates of the ClpP Protease in <i>Staphylococcus aureus</i>Semantic proximity Read ↗

The Spl Serine Proteases Modulate Staphylococcus aureus Protein Production and Virulence in a Rabbit Model of PneumoniaSemantic proximity Read ↗

A Chemical Disruptor of the ClpX Chaperone Complex Attenuates the Virulence of Multidrug‐Resistant Staphylococcus aureusSemantic proximity Read ↗

Characterization of Gain-of-Function Mutant Provides New Insights into ClpP Structure.Semantic proximity Read ↗

ClpX contributes to innate defense peptide resistance and virulence phenotypes of Bacillus anthracis.Semantic proximity Read ↗

Extracellular proteases are key mediators of <scp> <i>S</i> </scp> <i>taphylococcus aureus</i> virulence via the global modulation of virulence‐determinant stabilitySemantic proximity Read ↗

ClpX Is Essential and Activated by Single-Strand DNA Binding Protein in MycobacteriaSemantic proximity Read ↗

β-Lactam resistance in methicillin-resistant Staphylococcus aureus USA300 is increased by inactivation of the ClpXP protease.Semantic proximity Read ↗

The Protease SplB of Staphylococcus aureus Targets Host Complement Components and Inhibits Complement-Mediated Bacterial OpsonophagocytosisSemantic proximity Read ↗

Development of a New N-Terminomic Method to Study the Pathodegradome of the <i>Staphylococcus aureus</i> V8 Protease in Human NeutrophilsSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.