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A more recent version of this article appeared on February 15, 2008 Originally published In Press as doi:10.1074/jbc.M707917200 on November 20, 2007
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Papers In Press, published online ahead of print December 6, 2007
J. Biol. Chem, 10.1074/jbc.M707917200
Submitted on September 21, 2007
Revised on November 6, 2007
Accepted on November 20, 2007

Molecular architecture of Botulinum neurotoxin E revealed by single particle electron microscopy

Audrey Fischer, Consuelo Garcia-Rodriguez, Isin Geren, Jianlong Lou, James D. Marks, Terunaga Nakagawa, and Mauricio Montal

Division of Biological Sciences, Section of Neurobiology, UCSD, La Jolla, CA 92093-0366

Corresponding Author: mmontal{at}ucsd.edu

Clostridial botulinum neurotoxin (BoNT) causes a neuroparalytic condition recognized as botulism by arresting synaptic vesicle exocytosis. While the crystal structures of full-length BoNT/A and BoNT/B holotoxins are known, the molecular architecture of the five other serotypes remains elusive. Here, we present the structures of BoNT/A and BoNT/E using single-particle electron microscopy (EM). Labeling of the particles with three different monoclonal antibodies raised against BoNT/E revealed the positions of their epitopes in the EM structure, thereby identifying the three hallmark domains of BoNT (protease, translocation and receptor binding). Correspondingly, these antibodies selectively inhibit BoNT translocation activity as detected using a single-molecule assay. The global structure of BoNT/E is strikingly different from that of BoNT/A despite strong sequence similarity. We postulate that the unique architecture of functionally conserved modules underlies the distinguishing attributes of BoNT/E and contributes to differences with BoNT/A.


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J. Wang, J. Meng, G. W. Lawrence, T. H. Zurawski, A. Sasse, M. O. Bodeker, M. A. Gilmore, E. Fernandez-Salas, J. Francis, L. E. Steward, et al.
Novel Chimeras of Botulinum Neurotoxins A and E Unveil Contributions from the Binding, Translocation, and Protease Domains to Their Functional Characteristics
J. Biol. Chem., June 20, 2008; 283(25): 16993 - 17002.
[Abstract] [Full Text] [PDF]


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