Discover Community Create You

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 Intracellular Cyclophilin PpiB Contributes to the Virulence of Staphylococcus aureus Independently of Its Peptidyl-Prolyl cis/trans Isomerase Activity

14 Aug 2018

Abstract excerpt

The Staphylococcus aureus cyclophilin PpiB is an intracellular peptidyl prolyl cis/trans isomerase (PPIase) that has previously been shown to contribute to secreted nuclease and hemolytic activity. In this study, we investigated the contribution of PpiB to S. aureus virulence.

Read the complete abstract on PubMed

Topics

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

Share to Clostridium difficile and Clostridium perfringens research
Share to Signaling Pathways in Disease
Share to Toxin Mechanisms and Immunotoxins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Source

Identifiers

PMID: 30104214
DOI: 10.1128/iai.00379-18

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 10 closest

The Intracellular Cyclophilin PpiB Contributes to the Virulence of Staphylococcus aureus Independently of Its Peptidyl-Prolyl cis/trans Isomerase ActivityPMID 30104214Read ↗

An Intracellular Peptidyl-Prolyl cis/trans Isomerase Is Required for Folding and Activity of the Staphylococcus aureus Secreted Virulence Factor Nuclease.Semantic proximity Read ↗

Microbial Peptidyl-Prolyl <i>cis</i> / <i>trans</i> Isomerases (PPIases): Virulence Factors and Potential Alternative Drug TargetsSemantic proximity Read ↗

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

Characterisation of SEQ0694 (PrsA/PrtM) of Streptococcus equi as a functional peptidyl-prolyl isomerase affecting multiple secreted protein substrates.Semantic proximity Read ↗

Involvement of peptidylprolyl cis/trans isomerases in Enterococcus faecalis virulence.Semantic proximity Read ↗

Identification and comparative analysis of sixteen fungal peptidyl-prolyl cis/trans isomerase repertoiresSemantic proximity Read ↗

Solution structure of the parvulin-type PPIase domain of Staphylococcus aureus PrsA – Implications for the catalytic mechanism of parvulinsSemantic proximity Read ↗

Lif, the lysostaphin immunity factor, complements FemB in staphylococcal peptidoglycan interpeptide bridge formation.Semantic proximity Read ↗

Yeast cyclophilin-related gene encodes a nonessential second peptidyl-prolyl cis-trans isomerase associated with the secretory pathway.Semantic proximity Read ↗

Structural elucidation of the Cys‐His‐Glu‐Asn proteolytic relay in the secreted CHAP domain enzyme from the human pathogen <i>Staphylococcus saprophyticus</i>Semantic proximity Read ↗

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