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

Reversion of recombinant toxoids: mutations in diphtheria toxin that partially compensate for active-site deletions.

Proceedings of the National Academy of Sciences of the United States of America - 1 Jul 1992

Killeen K P, Escuyer V, Mekalanos J J, Collier R J

Abstract excerpt

Deleting an important active-site residue of diphtheria toxin, glutamic acid-148, reduces the toxin's ADP-ribosyltransferase activity by a factor of greater than 10(4). We considered using this mutation to construct a recombinant toxoid for expression by live attenuated vaccines and explored seco...

Topics

Amino Acid Sequence
Binding Sites
Diphtheria Toxin
Diphtheria Toxoid
Molecular Sequence Data
Mutagenesis, Site-Directed
Mutation
Poly(ADP-ribose) Polymerases
Protein Conformation
Recombinant Proteins
Structure-Activity Relationship

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Vaccines, Synthetic

Source

Open in PubMed Open full text

Identifiers

PMID: 1631110
DOI: 10.1073/pnas.89.13.6207
PMCID: PMC402151

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-1631110-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

Community interpretation

Discuss the evidence

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

0

discussions

0

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

Reversion of recombinant toxoids: mutations in diphtheria toxin that partially compensate for active-site deletions.PMID 1631110Read ↗

Selection of diphtheria toxin active-site mutants in yeast. Rediscovery of glutamic acid-148 as a key residue.Semantic proximity Read ↗

Mutations in diphtheria toxin to improve immunotoxin selectivity and understand toxin entry into cells.Semantic proximity Read ↗

Construction and expression of plasmids containing mutated diphtheria toxin A-chain-coding sequences.Semantic proximity Read ↗

Engineering of genetically detoxified pertussis toxin analogs for development of a recombinant whooping cough vaccine.Semantic proximity Read ↗

Active-site mutations of diphtheria toxin: role of tyrosine-65 in NAD binding and ADP-ribosylation.Semantic proximity Read ↗

Biochemical analysis of mutations at tyrosine-98 of the S1 subunit of pertussis toxin.Semantic proximity Read ↗

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

Gene replacement in Bordetella pertussis by transformation with linear DNA.Semantic proximity Read ↗

Uncoupling of GTP binding from target stimulation by a single mutation in the transducin alpha subunit.Semantic proximity Read ↗

Pseudomonas aeruginosa exotoxin A: alterations of biological and biochemical properties resulting from mutation of glutamic acid 553 to aspartic acid.Semantic proximity Read ↗

Structural basis for lack of toxicity of the diphtheria toxin mutant CRM197.Semantic proximity Read ↗

Targeted introduction of a diphtheria toxin resistant mutation into the chromosomal EF-2 locus of Pichia pastoris and expression of immunotoxin in the EF-2 mutants.Semantic proximity Read ↗

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