Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex-Reference-Cited by-同舟云学术

Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex

Published:2014-06-20 Issue:6190 Volume:344 Page:1405-1410
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Lee Kwangkook¹,Zhong Xiaofen²,Gu Shenyan¹,Kruel Anna Magdalena³,Dorner Martin B.⁴,Perry Kay⁵,Rummel Andreas³,Dong Min²,Jin Rongsheng¹

Affiliation:

1. Department of Physiology and Biophysics, University of California, Irvine, CA 92697, USA.

2. Department of Microbiology and Immunobiology, Harvard Medical School, Division of Neuroscience, New England Primate Research Center, Southborough, MA 01772, USA.

3. Institut für Toxikologie, Medizinische Hochschule Hannover, Carl-Neuberg-Strasse 1, 30625 Hannover, Germany.

4. Centre for Biological Threats and Special Pathogens–Biological Toxins (ZBS3), Robert Koch-Institut, Nordufer 20, 13353 Berlin, Germany.

5. Northeastern Collaborative Access Team (NE-CAT) and Department of Chemistry and Chemical Biology, Cornell University, Building 436E, Argonne National Laboratory, 9700 S. Cass Avenue, Argonne, IL 60439, USA.

Abstract

Breaking through the epithelial barrier Botulinum neurotoxin (BoNT) poisons its host when it crosses the intestinal epithelial barrier. To help it cross this barrier, the toxin forms a large complex with three bacterial proteins called hemagglutinins (HAs). To find out what happens when this complex binds to a cell-adhesion protein called E-cadherin, Lee et al. crystallized the bound complex and protein. Toxin binding disrupted the way E-cadherin maintains the epithelial barrier. When the researchers prevented the toxin complex from binding to E-cadherin, mice were protected from the toxin's deadly effects. Science , this issue p. 1405

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference42 articles.

1. Phylogeny and taxonomy of the food-borne pathogen Clostridium botulinum and its neurotoxins

2. Botulinum Neurotoxin Is Shielded by NTNHA in an Interlocked Complex

3. Oral toxicities of Clostridium botulinum toxins in response to molecular size

4. Oral toxicities of Clostridium botulinum type A and B toxins from different strains;Ohishi I.;Infect. Immun.,1984

Cited by 91 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Stable and efficient generation of functional iPSC-derived neural progenitor cell rosettes through regulation of collective cell-cell behavior;Frontiers in Bioengineering and Biotechnology;2024-01-10

2. Growth prolongation of human induced pluripotent stem cell aggregate in three-dimensional suspension culture system by addition of botulinum hemagglutinin;Journal of Bioscience and Bioengineering;2023-12

3. NTNH protein: more than a bodyguard for botulinum neurotoxins;The FEBS Journal;2023-11-27

4. No Secondary Treatment Failure during Incobotulinumtoxin—A Long-Term Treatment Demonstrated by the Drawing of Disease Severity;Toxins;2023-07-12

5. Pathogenicity and virulence of Clostridium botulinum;Virulence;2023-05-08