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Literature summary for 3.4.24.69 extracted from

  • Shone, C.; Agostini, H.; Clancy, J.; Gu, M.; Yang, H.H.; Chu, Y.; Johnson, V.; Taal, M.; McGlashan, J.; Brehm, J.; Tong, X.
    Bivalent recombinant vaccine for botulinum neurotoxin types A and B based on a polypeptide comprising their effector and translocation domains that is protective against the predominant A and B subtypes (2009), Infect. Immun., 77, 2795-2801.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.69

Application

Application Comment Organism
medicine LHN/A vaccine protects mice against challenge with BoNT/A subtypes A1, A2, and A3 Clostridium botulinum
medicine LHN/A vaccine protects mice against challenge with BoNT/A subtypes A1, A2, and A3,the LHN/B vaccine is also highly efficacious Clostridium botulinum
medicine LHN/B vaccine protects mice against challenge with BoNT/A subtypes A1, A2, and A3 Clostridium botulinum

Cloned(Commentary)

Cloned (Comment) Organism
catalytically inactive, mutated fragments, designated LHN, comprise the light chain and translocation domains of each neurotoxin and are devoid of any neuron-binding activity. Using codon-optimized genes, LHN fragments, derived from BoNT serotype A, are expressed in Escherichia coli in high yield as soluble proteins Clostridium botulinum
catalytically inactive, mutated fragments, designated LHN, comprise the light chain and translocation domains of each neurotoxin and are devoid of any neuron-binding activity. Using codon-optimized genes, LHN fragments, derived from BoNT serotype B, are expressed in Escherichia coli in high yield as soluble proteins Clostridium botulinum
catalytically inactive, mutated fragments, designated LHN, comprise the light chain and translocation domains of each neurotoxin and are devoid of any neuron-binding activity. Using codon-optimized genes, LHN fragments, derived from BoNT serotypes A and B, are expressed in Escherichia coli in high yield as soluble proteins Clostridium botulinum

Protein Variants

Protein Variants Comment Organism
E224Q/H227Y the mutation removes the endopeptidase activity of BoNT/A LH fragment Clostridium botulinum
E231Q/H234Y the mutation removes the endopeptidase activity of BoNT/B LH fragment Clostridium botulinum

Organism

Organism UniProt Comment Textmining
Clostridium botulinum P10844 BoNT/B
-
Clostridium botulinum P10844 BoNT/B; BoNT/A1, BoNT/A3, BoNT/B1, and BoNT/B4 from strains ATCC 3502, NCTC 2012, Okra, and Eklund 17B strains, respectively
-
Clostridium botulinum P10845 BoNT/A
-

Purification (Commentary)

Purification (Comment) Organism
native BoNT/A1 and BoNT/A3, by ultrafiltration, hydrophobic interaction and anion exchange chromatography, followed by hydroxyapatite chromatography and dialysis Clostridium botulinum
native BoNT/A1, BoNT/A3, BoNT/B1, and BoNT/B4 from strains ATCC 3502, NCTC 2012, Okra, and Eklund 17B strains, respectively, by ultrafiltration, hydrophobic interaction and anion exchange chromatography, followed by hydroxyapatite chromatography and dialysis Clostridium botulinum
native BoNT/B1, and BoNT/B4 by ultrafiltration, hydrophobic interaction and anion exchange chromatography, followed by hydroxyapatite chromatography and dialysis Clostridium botulinum

Subunits

Subunits Comment Organism
More enzyme model with light chain LC or effector domain, showing the catalytic activity, heavy chain HC binding domain binding to neuronal receptors, after which the HN translocation domain mediates the entry of the light chain into the nerve cell Clostridium botulinum

Synonyms

Synonyms Comment Organism
BoNT/A
-
 Clostridium botulinum
BoNT/B
-
 Clostridium botulinum
botulinum neurotoxin type A
-
 Clostridium botulinum
botulinum neurotoxin type B
-
 Clostridium botulinum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Clostridium botulinum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Clostridium botulinum