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

Identification and characterisation a surface-associated arginine peptidase in Streptococcus suis serotype 2.

Microbiological research - 1 Jan 2015

Huang Kaisong, Yuan Zengzhi, Li Jingtao, Zhang Qiang, Xu Zhongmin, Yan Shuxian, Zhang Anding, Jin Meilin

Abstract excerpt

Streptococcus suis is an important zoonotic pathogen worldwide and is responsible for disease in swine and humans. In the present study, we identified and characterised a surface-associated peptidase (abpb, amylase-binding protein B) in Streptococcus suis serotype 2 (S. suis 2) that has high hydrolytic activity towards H-Arg-pNa, with maximum activity at pH 7.0. Stimulation of RAW 264.7 macrophages with purified...

Read the complete abstract on PubMed

Topics

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

Share to Cell Wall
Share to Endopeptidases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gene Order

Share to Genetic Vectors

Share to Inflammation Mediators

Share to Serogroup

Share to Streptococcal Infections

Share to Streptococcus suis

Source

Identifiers

PMID: 25179447
DOI: 10.1016/j.micres.2014.08.001

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification and characterisation a surface-associated arginine peptidase in Streptococcus suis serotype 2.PMID 25179447Read ↗

Peptidomics Analysis of Virulent Peptides Involved in Streptococcus suis PathogenesisSemantic proximity Read ↗

Surface-associated and secreted factors of<i>Streptococcus suis</i>in epidemiology, pathogenesis and vaccine developmentSemantic proximity Read ↗

Identification of a cell wall-associated subtilisin-like serine protease involved in the pathogenesis of Streptococcus suis serotype 2Semantic proximity Read ↗

A novel endolysin disruptsStreptococcus suiswith high efficiencySemantic proximity Read ↗

Flanking N- and C-terminal domains of PrsA in Streptococcus suis type 2 are crucial for inducing cell death independent of TLR2 recognitionSemantic proximity Read ↗

YSIRK-G/S-directed translocation is required for Streptococcus suis to deliver diverse cell wall anchoring effectors contributing to bacterial pathogenicitySemantic proximity Read ↗

How Streptococcus suis serotype 2 attempts to avoid attack by host immune defensesSemantic proximity Read ↗

Structural and Functional Analysis of Cell Wall-anchored Polypeptide Adhesin BspA in Streptococcus agalactiaeSemantic proximity Read ↗

Identification of oligopeptide-binding protein (OppA) and its role in the virulence of Streptococcus suis serotype 2Semantic proximity Read ↗

Subtilisin-like protease-1 secreted through type IV secretion system contributes to high virulence of Streptococcus suis 2Semantic proximity Read ↗

Bacterial serine proteases secreted by the autotransporter pathway: classification, specificity, and role in virulence.Semantic proximity Read ↗

Comparative proteomic analyses of Streptococcus suis serotype 2 cell wall-associated proteins.Semantic proximity Read ↗

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