Amino-terminal domain of the El Tor haemolysin of Vibrio cholerae O1 is expressed in classical strains and is cytotoxic.

doi:10.1016/0264-410x(91)90247-4

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

Back to search

Article

Amino-terminal domain of the El Tor haemolysin of Vibrio cholerae O1 is expressed in classical strains and is cytotoxic.

Vaccine - 1 Aug 1991

Alm R A, Mayrhofer G, Kotlarski I, Manning P A

Abstract excerpt

Previous studies have shown that the classical isolates of Vibrio cholerae possess an 11 bp deletion in the structural gene for the El Tor haemolysin leading to the production of a 27 kDa non-haemolytic truncated product HlyA* compared to the 82 kDa haemolysin, HlyA. These studies were designed to assess whether this truncated product had any biological activity. A KmR cartridge was introduced into the hlyA gene...

Topics

Animals
Bacterial Proteins
Body Water
Cell Survival
Electrophoresis, Polyacrylamide Gel
Escherichia coli Proteins
Gene Expression
Hemolysin Proteins
Humans
Ileum
Mice

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Nucleic Acid Hybridization

Plasmids

Tumor Cells, Cultured

Vibrio cholerae

Virulence

Source

Open in PubMed

Identifiers

PMID: 1771972
DOI: 10.1016/0264-410x(91)90247-4

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1771972-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Amino-terminal domain of the El Tor haemolysin of Vibrio cholerae O1 is expressed in classical strains and is cytotoxic.PMID 1771972Read ↗

Characterization of the hlyB gene and its role in the production of the El Tor haemolysin of Vibrio cholerae O1.Semantic proximity Read ↗

Cloning and characterization of a novel haemolysin in Vibrio cholerae O1 that does not directly contribute to the virulence of the organism.Semantic proximity Read ↗

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

The deletion of several amino acid stretches of Escherichia coli alpha-hemolysin (HlyA) suggests that the channel-forming domain contains beta-strands.Semantic proximity Read ↗

Conversion of Vibrio eltor MAK757 to classical biotype: role of phage PS166.Semantic proximity Read ↗

Mutational analysis supports a role for multiple structural features in the C-terminal secretion signal of Escherichia coli haemolysin.Semantic proximity Read ↗

Aberrant gene for E1 Tor hemolysin from Vibrio cholerae non-O1, N037.Semantic proximity Read ↗

Mutations affecting export and activity of cytolysin A from Escherichia coli.Semantic proximity Read ↗

Culture supernatants from V. cholerae O1 El Tor strains isolated from different geographic areas induce cell vacuolation and cytotoxicity.Semantic proximity Read ↗

Analysis of toxinogenic functions associated with the RTX repeat region and monoclonal antibody D12 epitope of Escherichia coli hemolysin.Semantic proximity Read ↗

Molecular analysis of bacterial cytolysins.Semantic proximity Read ↗

Mutations affecting the extreme C terminus of Escherichia coli haemolysin A reduce haemolytic activity by altering the folding of the toxin.Semantic proximity Read ↗

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