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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Veröffentlicht in:	Proc Natl Acad Sci U S A
Hauptverfasser:	Streatfield, S J, Sandkvist, M, Sixma, T K, Bagdasarian, M, Hol, W G, Hirst, T R
Format:	Artigo
Sprache:	Inglês
Veröffentlicht:	National Academy of Sciences 1992
Schlagworte:	Research Article
Online-Zugang:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC50714/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/1465452/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.89.24.12140
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