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-Structure paper
タイトル | Glycan-dependent cell adhesion mechanism of Tc toxins. |
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ジャーナル・号・ページ | Nat Commun, Vol. 11, Issue 1, Page 2694, Year 2020 |
掲載日 | 2020年6月1日 |
著者 | Daniel Roderer / Felix Bröcker / Oleg Sitsel / Paulina Kaplonek / Franziska Leidreiter / Peter H Seeberger / Stefan Raunser / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:32483155 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.2 - 5.0 Å |
構造データ | EMDB-10794: EMDB-10796, PDB-6yew: EMDB-10797, PDB-6yey: |
由来 |
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キーワード | TOXIN / complex / glycan |