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

Protective capacities of cell surface-associated proteins of Streptococcus suis mutants deficient in divalent cation-uptake regulators.

Microbiology (Reading, England) - 1 May 2009

Aranda Jesús, Garrido Maria Elena, Fittipaldi Nahuel, Cortés Pilar, Llagostera Montserrat, Gottschalk Marcelo, Barbé Jordi

Abstract excerpt

Many cell surface-associated, divalent cation-regulated proteins are immunogenic, and some of them confer protection against the bacterial species from which they are derived. In this work, two Streptococcus suis divalent cation uptake regulator genes controlling zinc/manganese and iron uptake (adcR and fur, respectively) were inactivated in order to study the protective capacities of their cell...

Read the complete abstract on PubMed

Topics

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

Share to Biological Transport
Share to Cations, Divalent

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gene Expression Regulation, Bacterial

Share to Membrane Proteins

Share to Mice, Inbred BALB C

Share to Repressor Proteins

Share to Streptococcal Infections

Share to Streptococcus suis

Source

Identifiers

PMID: 19372168
DOI: 10.1099/mic.0.026278-0

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Protective capacities of cell surface-associated proteins of Streptococcus suis mutants deficient in divalent cation-uptake regulators.PMID 19372168Read ↗

Analysis of the Protective Capacity of ThreeStreptococcus suisProteins Induced under Divalent-Cation-Limited ConditionsSemantic proximity Read ↗

Group A Streptococcus AdcR Regulon Participates in Bacterial Defense against Host-Mediated Zinc Sequestration and Contributes to VirulenceSemantic proximity Read ↗

The role of zinc in the interplay between pathogenic streptococci and their hostsSemantic proximity Read ↗

A Critical Role of Zinc Importer AdcABC in Group A Streptococcus-Host Interactions During Infection and Its Implications for Vaccine DevelopmentSemantic proximity Read ↗

Identification of zinc-dependent mechanisms used by Group B <i>Streptococcus</i> to overcome calprotectin-mediated stressSemantic 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 ↗

Pneumococcal histidine triad proteins are regulated by the Zn2+-dependent repressor AdcR and inhibit complement deposition through the recruitment of complement factor H.Semantic proximity Read ↗

AdcAII of Streptococcus pneumoniae Affects Pneumococcal Invasiveness.Semantic proximity Read ↗

The AdcACB/AdcAII system is essential for zinc homeostasis and an important contributor of Enterococcus faecalis virulenceSemantic proximity Read ↗

Comparative genomics of bacterial zinc regulons: Enhanced ion transport, pathogenesis, and rearrangement of ribosomal proteinsSemantic proximity Read ↗

Non-cognate immunity proteins provide broader defenses against interbacterial effectors in microbial communitiesSemantic proximity Read ↗

Zinc’ing it out: zinc homeostasis mechanisms and their impact on the pathogenesis of human pathogen group A streptococcusSemantic proximity Read ↗

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