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 Role of the Exopolyphosphatase PPX in Avoidance by Neisseria meningitidis of Complement-mediated Killing

25 Aug 2010

Abstract excerpt

The complement system is critical for immunity against the important human pathogen Neisseria meningitidis. We describe the isolation of a meningococcal mutant lacking PPX, an exopolyphosphatase responsible for cleaving cellular polyphosphate, a polymer of tens to hundreds of orthophosphate residues found in virtually all living cells. Bacteria lacking PPX exhibit increased resistance to complement-mediated...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Infections and Vaccines
Share to Coagulation, Bradykinin, Polyphosphates, and Angioedema
Share to Complement system in diseases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 20736171
DOI: 10.1074/jbc.m110.154393

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 · 12 closest

The Role of the Exopolyphosphatase PPX in Avoidance by Neisseria meningitidis of Complement-mediated KillingPMID 20736171Read ↗

The role of exopolyphosphatase in Neisseria meningitidis infectionSemantic proximity Read ↗

PepN is a non-essential, cell wall-localized protein that contributes to neutrophil elastase-mediated killing of <i>Streptococcus pneumoniae</i>Semantic proximity Read ↗

Interactions between Neisseria meningitidis and the complement system.Semantic proximity Read ↗

<i>Streptococcus pyogenes</i> nuclease A interferes with host complement functionsSemantic proximity Read ↗

Streptococcus pyogenes Endopeptidase O Contributes to Evasion from Complement-mediated Bacteriolysis via Binding to Human Complement Factor C1qSemantic proximity Read ↗

Polyphosphatases have a polyphosphate-independent influence on the virulence of Cryptococcus neoformansSemantic proximity Read ↗

Neisseria meningitidis NalP cleaves human complement C3, facilitating degradation of C3b and survival in human serum.Semantic proximity Read ↗

A highly conserved interaction involving the middle residue of the SXN active-site motif is crucial for function of class B penicillin-binding proteins: mutational and computational analysis of PBP 2 from N. gonorrhoeae.Semantic proximity Read ↗

Generation and characterization of a PhoP homologue mutant of Neisseria meningitidis.Semantic proximity Read ↗

The type II O‐antigenic polysaccharide moiety of <i>Burkholderia pseudomallei</i> lipopolysaccharide is required for serum resistance and virulenceSemantic proximity Read ↗

Alanine 501 Mutations in Penicillin-Binding Protein 2 from Neisseria gonorrhoeae: Structure, Mechanism, and Effects on Cephalosporin Resistance and Biological Fitness.Semantic proximity Read ↗

Structure-Function Studies of the Neisseria gonorrhoeae Major Outer Membrane PorinSemantic proximity Read ↗

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