Intermolecular interactions between the A and B subunits of heat-labile enterotoxin from Escherichia coli promote holotoxin assembly and stability in vivo.

Cholera toxin and the related heat-labile enterotoxin (LT) produced by Escherichia coli consist of a holotoxin of one A subunit and five B subunits (AB5). Here we investigate the domains of the A subunit (EtxA) of E. coli LT which influence the events of B-subunit (EtxB) oligomerization and the form...

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Hauptverfasser: Streatfield, S J, Sandkvist, M, Sixma, T K, Bagdasarian, M, Hol, W G, Hirst, T R
Format: Artigo
Sprache:Inglês
Veröffentlicht: 1992
Schlagworte:
Research Article
Online Zugang:https://ncbi.nlm.nih.gov/pmc/articles/PMC50714/
https://ncbi.nlm.nih.gov/pubmed/1465452
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