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 H35A mutated alpha-toxin interferes with cytotoxicity of staphylococcal alpha-toxin.

Infection and immunity - 1 Mar 2009

Liang Xudong, Yan Meiying, Ji Yinduo

Abstract excerpt

Staphylococcal alpha-toxin is an important virulence factor for Staphylococcus aureus to cause severe infections. In this study, we explored whether the toxoid of alpha-toxin may be utilized to block the toxicity of wild-type alpha-toxin. We created a series of H35A mutated alpha-toxin expression strains and revealed that the H35A mutation eliminates the activity of alpha-toxin using a human lung epithelial cell...

Read the complete abstract on PubMed

Topics

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

Share to Cell Line
Share to Fluorescent Antibody Technique
Share to Mutagenesis, Site-Directed

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Pore Forming Cytotoxic Proteins

Share to Staphylococcal Infections

Share to Staphylococcus aureus

Share to Virulence Factors

Source

Open in PubMed Open full text

Identifiers

PMID: 19103771
DOI: 10.1128/IAI.00920-08
PMCID: PMC2643624

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

The H35A mutated alpha-toxin interferes with cytotoxicity of staphylococcal alpha-toxin.PMID 19103771Read ↗

Staphylococcus aureus α-Toxin: Nearly a Century of IntrigueSemantic proximity Read ↗

Targeting Staphylococcus aureus Toxins: A Potential form of Anti-Virulence TherapySemantic proximity Read ↗

Bacterial Toxins: Friends or Foes?Semantic proximity Read ↗

Alanine scanning mutagenesis of the MEDI4839 (Suvratoxumab) epitope reduces alpha toxin lytic activity <i>in vitro</i> and <i>S. aureus</i> fitness in infection modelsSemantic proximity Read ↗

Alanine Scanning Mutagenesis of the MEDI4893 (Suvratoxumab) Epitope Reduces Alpha Toxin Lytic Activity In Vitro and Staphylococcus aureus Fitness in Infection ModelsSemantic proximity Read ↗

Functional and Structural Insights of a Staphylococcus aureus Apoptotic-like Membrane Peptide from a Toxin-Antitoxin ModuleSemantic proximity Read ↗

Genome-wide CRISPR screen reveals novel host factors required for Staphylococcus aureus α-hemolysin-mediated toxicitySemantic proximity Read ↗

Elimination of a bacterial pore-forming toxin by sequential endocytosis and exocytosis.Semantic proximity Read ↗

Novel toxic shock syndrome toxin-1 amino acids required for biological activity.Semantic proximity Read ↗

Auto-Assembling Detoxified Staphylococcus aureus Alpha-Hemolysin Mimicking the Wild-Type Cytolytic ToxinSemantic proximity Read ↗

Identification of functional domains of Clostridium septicum alpha toxin.Semantic proximity Read ↗

Autophagy Mediates Tolerance to Staphylococcus aureus Alpha-ToxinSemantic proximity Read ↗

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