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  Glycan-dependent cell adhesion mechanism of Tc toxins

Roderer, D., Bröcker, F., Sitsel, O., Kapłonek, P., Leidreiter, F., Seeberger, P. H., et al. (2020). Glycan-dependent cell adhesion mechanism of Tc toxins. Nature Communications, 11: 2694. doi:10.1038/s41467-020-16536-7.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0006-866C-A Version Permalink: http://hdl.handle.net/21.11116/0000-0006-866D-9
Genre: Journal Article

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 Creators:
Roderer, Daniel, Author
Bröcker, Felix1, Author              
Sitsel, Oleg, Author
Kapłonek, Paulina1, Author              
Leidreiter, Franziska, Author
Seeberger, Peter H.1, Author              
Raunser, Stefan, Author
Affiliations:
1Peter H. Seeberger - Vaccine Development, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863308              

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 Abstract: Toxin complex (Tc) toxins are virulence factors of pathogenic bacteria. Tcs are composed of three subunits: TcA, TcB and TcC. TcA facilitates receptor–toxin interaction and membrane permeation, TcB and TcC form a toxin-encapsulating cocoon. While the mechanisms of holotoxin assembly and pore formation have been described, little is known about receptor binding of TcAs. Here, we identify heparins/heparan sulfates and Lewis antigens as receptors for different TcAs from insect and human pathogens. Glycan array screening reveals that all tested TcAs bind negatively charged heparins. Cryo-EM structures of Morganella morganii TcdA4 and Xenorhabdus nematophila XptA1 reveal that heparins/heparan sulfates unexpectedly bind to different regions of the shell domain, including receptor-binding domains. In addition, Photorhabdus luminescens TcdA1 binds to Lewis antigens with micromolar affinity. Here, the glycan interacts with the receptor-binding domain D of the toxin. Our results suggest a glycan dependent association mechanism of Tc toxins on the host cell surface.

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Language(s): eng - English
 Dates: 2020-06-012020
 Publication Status: Published in print
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 Identifiers: DOI: 10.1038/s41467-020-16536-7
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Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 11 Sequence Number: 2694 Start / End Page: - Identifier: ISSN: 2041-1723