Host glycan recognition by a pore forming toxin
- PMID: 22325766
- PMCID: PMC3279720
- DOI: 10.1016/j.str.2012.01.013
Host glycan recognition by a pore forming toxin
Abstract
An exposed F-type lectin domain fused to the N-terminus of a cholesterol-dependent cytolysin scaffold allows Streptococcus mitis lectinolysin to cluster at fucose-rich sites on target cell membranes, thereby leading to increased pore-forming toxin activity. In this issue of Structure, Feil and coworkers define the structural basis for lectinolysin glycan-binding specificity.
Copyright © 2012 Elsevier Ltd. All rights reserved.
Comment on
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Structure of the lectin regulatory domain of the cholesterol-dependent cytolysin lectinolysin reveals the basis for its lewis antigen specificity.Structure. 2012 Feb 8;20(2):248-58. doi: 10.1016/j.str.2011.11.017. Structure. 2012. PMID: 22325774 Free PMC article.
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- Feil, et al. Structure. 2012;20:xxx–xxxx.
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- Giddings KS, Zhao J, Sims PJ, Tweten RK. Hum. CD59 is a Receptor for the Cholesterol-Dependent Cytolysin Intermedilysin. Nat. Struct. Mol. Biol. 2004;12:1173–1178. - PubMed
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