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 variant undecapeptide sequence of the Arcanobacterium pyogenes haemolysin, pyolysin, is required for full cytolytic activity.

Microbiology (Reading, England) - 1 Dec 2002

Billington Stephen J, Songer J Glenn, Jost B Helen

Abstract excerpt

The cholesterol-dependent cytolysins (CDCs) are characterized by an undecapeptide sequence (ECTGLAWEWWR) that is located near the C terminus and within domain 4 of these proteins. Pyolysin (PLO), the CDC of Arcanobacterium pyogenes, has a variant undecapeptide sequence (EATGLAWDPWW). Site-directed mutants were constructed in undecapeptide residues in a recombinant PLO molecule containing a hexahistidine tag...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Substitution
Share to Bacterial Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Bacterial Toxins

Share to Cholesterol

Share to Hemolysin Proteins

Share to Hemolysis

Share to Mutagenesis, Site-Directed

Share to Virulence

Source

Identifiers

PMID: 12480898
DOI: 10.1099/00221287-148-12-3947

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The variant undecapeptide sequence of the Arcanobacterium pyogenes haemolysin, pyolysin, is required for full cytolytic activity.PMID 12480898Read ↗

Pneumolysin: Pathogenesis and Therapeutic TargetSemantic proximity Read ↗

Replacing the 238th aspartic acid with an arginine impaired the oligomerization activity and inflammation-inducing property of pyolysin.Semantic proximity Read ↗

A Key Motif in the Cholesterol-Dependent Cytolysins Reveals a Large Family of Related ProteinsSemantic proximity Read ↗

Pneumolysin: A Double-Edged Sword During the Host-Pathogen InteractionSemantic proximity Read ↗

Structure-based functional studies for the cellular recognition and cytolytic mechanism of pneumolysin from Streptococcus pneumoniae.Semantic proximity Read ↗

Escherichia coli hemolysin mutants with altered target cell specificity.Semantic proximity Read ↗

Crystal structure of cytotoxin protein suilysin from Streptococcus suisSemantic proximity Read ↗

The cholesterol-dependent cytolysin pneumolysin from Streptococcus pneumoniae binds to lipid raft microdomains in human corneal epithelial cells.Semantic proximity Read ↗

Partial oligomerization of pyolysin induced by a disulfide-tethered mutant.Semantic proximity Read ↗

Preferential modification of CyaA-hemolysin by CyaC-acyltransferase through the catalytic Ser30-His33 dyad in esterolysis of palmitoyl-donor substrate devoid of acyl carrier proteins.Semantic proximity Read ↗

Structure–Activity Relationships of the Enterococcal CytolysinSemantic proximity Read ↗

Perfringolysin O structure and mechanism of pore formation as a paradigm for cholesterol-dependent cytolysins.Semantic proximity Read ↗

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