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

Mutations in the A subunit affect yield, stability, and protease sensitivity of nontoxic derivatives of heat-labile enterotoxin.

Infection and immunity - 1 Dec 1996

Magagnoli C, Manetti R, Fontana M R, Giannelli V, Giuliani M M, Rappuoli R, Pizza M

Abstract excerpt

Heat-labile toxin (LT) is a protein related to cholera toxin, produced by enterotoxigenic Escherichia coli strains, that is organized as an AB5 complex. A number of nontoxic derivatives of LT, useful for new or improved vaccines against diarrheal diseases or as mucosal adjuvants, have been constructed by site-directed mutagenesis. Here we have studied the biochemical properties of the nontoxic mutants LT-K7...

Read the complete abstract on PubMed

Topics

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

Share to Endopeptidases
Share to Enterotoxins

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

Share to Escherichia coli

Share to Hot Temperature

Share to Mutation

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 8945604
DOI: 10.1128/iai.64.12.5434-5438.1996
PMCID: PMC174546

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

Mutations in the A subunit affect yield, stability, and protease sensitivity of nontoxic derivatives of heat-labile enterotoxin.PMID 8945604Read ↗

Protease susceptibility and toxicity of heat-labile enterotoxins with a mutation in the active site or in the protease-sensitive loop.Semantic proximity Read ↗

Construction of nontoxic derivatives of cholera toxin and characterization of the immunological response against the A subunit.Semantic proximity Read ↗

Mutants of the Escherichia coli heat-labile enterotoxin as safe and strong adjuvants for intranasal delivery of vaccines.Semantic proximity Read ↗

Non-toxic derivatives of LT as potent adjuvants.Semantic proximity Read ↗

Biological and biochemical characterization of variant A subunits of cholera toxin constructed by site-directed mutagenesis.Semantic proximity Read ↗

Mucosal vaccines: non toxic derivatives of LT and CT as mucosal adjuvants.Semantic proximity Read ↗

Functional Diversity of Heat-labile Toxins (LT) Produced by Enterotoxigenic Escherichia coliSemantic proximity Read ↗

Genetic detoxification and adjuvant-activity retention of Escherichia coli enterotoxin LT.Semantic proximity Read ↗

Mutants of Escherichia coli heat-labile enterotoxin as an adjuvant for nasal influenza vaccine.Semantic proximity Read ↗

Secretory and GM1 receptor binding role of N-terminal region of LTB in Vibrio cholerae.Semantic proximity Read ↗

Mutants of the Escherichia coli heat-labile enterotoxin with reduced ADP-ribosylation activity or no activity retain the immunogenic properties of the native holotoxin.Semantic proximity Read ↗

New insights into the structure-function relationships and therapeutic applications of cholera-like enterotoxins.Semantic proximity Read ↗

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