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

Pneumococcal zinc metalloproteinase ZmpC cleaves human matrix metalloproteinase 9 and is a virulence factor in experimental pneumonia.

Molecular microbiology - 1 Aug 2003

Oggioni Marco R, Memmi Guido, Maggi Tiziana, Chiavolini Damiana, Iannelli Francesco, Pozzi Gianni

Abstract excerpt

The ZmpC zinc metalloproteinase of Streptococcus pneumoniae, annotated in the type 4 genome as SP0071, was found to cleave human matrix metalloproteinase 9 (MMP-9). The previously described IgA protease activity was confirmed to be specifically linked to the IgA1-protease/SP1154 zinc metalloproteinase. MMP-9 is a protease cleaving extracellular matrix gelatin and collagen and is activated by proteolytic cleavage...

Read the complete abstract on PubMed

Topics

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

Share to Administration, Intranasal
Share to Blood-Brain Barrier

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Body Fluids

Share to Extracellular Matrix

Share to Matrix Metalloproteinase 9

Share to Metalloendopeptidases

Share to Pneumonia, Pneumococcal

Share to Streptococcus pneumoniae

Source

Identifiers

PMID: 12864860
DOI: 10.1046/j.1365-2958.2003.03596.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Pneumococcal zinc metalloproteinase ZmpC cleaves human matrix metalloproteinase 9 and is a virulence factor in experimental pneumonia.PMID 12864860Read ↗

The role of ZmpC in the clinical manifestation of invasive pneumococcal disease.Semantic proximity Read ↗

The three extra-cellular zinc metalloproteinases of Streptococcus pneumoniae have a different impact on virulence in miceSemantic proximity Read ↗

Occurrence and Evolution of the Paralogous Zinc Metalloproteases IgA1 Protease, ZmpB, ZmpC, and ZmpD in Streptococcus pneumoniae and Related Commensal SpeciesSemantic proximity Read ↗

Pathogenicity and virulence of Streptococcus pneumoniae : Cutting to the chase on proteasesSemantic proximity Read ↗

Identification, cloning, and sequencing of the immunoglobulin A1 protease gene of Streptococcus pneumoniaeSemantic proximity Read ↗

ZmpB, a novel virulence factor of Streptococcus pneumoniae that induces tumor necrosis factor alpha production in the respiratory tract.Semantic proximity Read ↗

<i>Streptococcus pyogenes</i> SpyCEP: a chemokine‐inactivating protease with unique structural and biochemical featuresSemantic proximity Read ↗

<scp>AdcA</scp> and <scp>AdcAII</scp> employ distinct zinc acquisition mechanisms and contribute additively to zinc homeostasis in <scp><i>S</i></scp><i>treptococcus pneumoniae</i>Semantic proximity Read ↗

A conserved Streptococcus pyogenes extracellular cysteine protease cleaves human fibronectin and degrades vitronectin.Semantic proximity Read ↗

Streptococcus pneumoniae endopeptidase O (PepO) is a multifunctional plasminogen- and fibronectin-binding protein, facilitating evasion of innate immunity and invasion of host cells.Semantic proximity Read ↗

Associations of MMP9 polymorphism with the risk of severe pneumonia in a Southern Chinese children population.Semantic proximity Read ↗

Streptococcus pyogenes Infection and the Human Proteome with a Special Focus on the Immunoglobulin G-cleaving Enzyme IdeSSemantic proximity Read ↗

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