Earlier this year I ran into a barfblog reader who said, ‘You’re really scared of botulism, aren’t you?’

The question was was related to a few things I had posted about the 24 illnesses and a death linked to an Ohio church potluck dinner. Improperly home canned potatoes were implicated.

I dunno about scared, maybe just in awe. The toxin blocks motor nerve terminals at the myoneural junction, causing paralysis. It starts with the mouth, eyes, face and moves down through the body. It often results in paralysis of the chest muscles and diaphragm, making a ventilator necessary. Months of recovery follow an intoxication.

Maybe I am scared.

Today researchers from the Brookhaven National Laboratories published research in Nature Scientific Reports about how one of the neurotoxins produced by Clostridium botulinum is protected in certain environments – info that can provide insight into vaccination and post-exposure mitigation.

Molecular Assembly of Clostridium botulinum progenitor M complex of type E

Nature Scientific Reports | 5:17795 | DOI: 10.1038/srep17795

Subramaniam Eswaramoorthy, Jingchuan Sun, Huilin Li, Bal Ram Singh & Subramanyam Swaminathan

Clostridium botulinum neurotoxin (BoNT) is released as a progenitor complex, in association with a non-toxic-non-hemagglutinin protein (NTNH) and other associated proteins. We have determined the crystal structure of M type Progenitor complex of botulinum neurotoxin E [PTC-E(M)], a heterodimer of BoNT and NTNH. The crystal structure reveals that the complex exists as a tight, interlocked heterodimer of BoNT and NTNH. The crystal structure explains the mechanism of molecular assembly of the complex and reveals several acidic clusters at the interface responsible for association at low acidic pH and disassociation at basic/neutral pH. The similarity of the general architecture between the PTC-E(M) and the previously determined PTC-A(M) strongly suggests that the progenitor M complexes of all botulinum serotypes may have similar molecular arrangement, although the neurotoxins apparently can take very different conformation when they are released from the M complex.