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 channel-forming toxin aerolysin neutralizes human immunodeficiency virus type 1.

Molecular microbiology - 1 Aug 1999

Nguyen D H, Liao Z, Buckley J T, Hildreth J E

Abstract excerpt

Aerolysin is a channel-forming toxin secreted by Aeromonas spp. that binds to glycosyl phosphatidylinositol (GPI)-anchored proteins, such as Thy-1, on sensitive target cells. Receptor binding is followed first by oligomerization of the toxin and then by insertion of the oligomers into the membrane to form stable channels that disrupt the permeability barrier. Human immunodeficiency virus type 1 (HIV-1) produced...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Toxins
Share to Glycosylphosphatidylinositols
Share to Ion Channels

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Jurkat Cells

Share to Phosphatidylinositol Diacylglycerol-Lyase

Share to Phosphoinositide Phospholipase C

Share to Pore Forming Cytotoxic Proteins

Share to Type C Phospholipases

Source

Identifiers

PMID: 10417655
DOI: 10.1046/j.1365-2958.1999.01518.x

Genes

GPI

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

The channel-forming toxin aerolysin neutralizes human immunodeficiency virus type 1.PMID 10417655Read ↗

A rivet model for channel formation by aerolysin-like pore-forming toxins.Semantic proximity Read ↗

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

Generation and characterization of Clostridium septicum alpha toxin mutants and their use in diagnosing paroxysmal nocturnal hemoglobinuria.Semantic proximity Read ↗

Site-directed mutagenesis of the hole-forming toxin aerolysin: studies on the roles of histidines in receptor binding and oligomerization of the monomer.Semantic proximity Read ↗

The H35A mutated alpha-toxin interferes with cytotoxicity of staphylococcal alpha-toxin.Semantic proximity Read ↗

Aerolysin, a hemolysin from Aeromonas hydrophila, forms voltage-gated channels in planar lipid bilayers.Semantic proximity Read ↗

Characterization of envelope glycoprotein mutants for human T-cell leukemia virus type 1 infectivity and immortalization.Semantic proximity Read ↗

MARTX toxin of Vibrio vulnificus induces RBC phosphatidylserine exposure that can contribute to thrombosisSemantic proximity Read ↗

Single-molecule sensing of peptides and nucleic acids by engineered aerolysin nanopores.Semantic proximity Read ↗

Imaging oligomers of alpha-toxin (Hla) variants using high-speed AFM and neutralizing Hla hemolytic activity with their antisera.Semantic proximity Read ↗

Dimer dissociation of the pore-forming toxin aerolysin precedes receptor binding.Semantic proximity Read ↗

Purification of cloned proaerolysin released by a low protease mutant of Aeromonas salmonicida.Semantic proximity Read ↗

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