NMR study of mutations of glycine-52 of the catalytic domain of diphtheria toxin.

doi:10.1016/j.jpba.2017.11.056

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

NMR study of mutations of glycine-52 of the catalytic domain of diphtheria toxin.

Journal of pharmaceutical and biomedical analysis - 20 Feb 2018

Sauvé Simon, Gingras Geneviève, Aubin Yves

Abstract excerpt

Cross-reacting-material 197 (CRM197) is a naturally occurring non-toxic mutant of diphtheria toxin (DT) that is one of the few carrier protein used in the manufacture of polysaccharide vaccines targeting bacterial pathogens such as Neisseria meningitidis, Streptococcus pneumaniae and Haemophilus influenzae. A detailed explanation in structural terms for the lack of toxicity has started to emerge with the report...

Topics

Amino Acid Substitution
Bacterial Proteins
Catalytic Domain
Glycine
Magnetic Resonance Spectroscopy
Mutation

Source

Open in PubMed

Identifiers

PMID: 29216588
DOI: 10.1016/j.jpba.2017.11.056

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 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.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics