Structural basis for receptor recognition and pore formation of a zebrafish aerolysin-like protein.

Abstract:

:Various aerolysin-like pore-forming proteins have been identified from bacteria to vertebrates. However, the mechanism of receptor recognition and/or pore formation of the eukaryotic members remains unknown. Here, we present the first crystal and electron microscopy structures of a vertebrate aerolysin-like protein from Danio rerio, termed Dln1, before and after pore formation. Each subunit of Dln1 dimer comprises a β-prism lectin module followed by an aerolysin module. Specific binding of the lectin module toward high-mannose glycans triggers drastic conformational changes of the aerolysin module in a pH-dependent manner, ultimately resulting in the formation of a membrane-bound octameric pore. Structural analyses combined with computational simulations and biochemical assays suggest a pore-forming process with an activation mechanism distinct from the previously characterized bacterial members. Moreover, Dln1 and its homologs are ubiquitously distributed in bony fishes and lamprey, suggesting a novel fish-specific defense molecule.

journal_name

EMBO Rep

journal_title

EMBO reports

authors

Jia N,Liu N,Cheng W,Jiang YL,Sun H,Chen LL,Peng J,Zhang Y,Ding YH,Zhang ZH,Wang X,Cai G,Wang J,Dong MQ,Zhang Z,Wu H,Wang HW,Chen Y,Zhou CZ

doi

10.15252/embr.201540851

subject

Has Abstract

pub_date

2016-02-01 00:00:00

pages

235-48

issue

2

eissn

1469-221X

issn

1469-3178

pii

embr.201540851

journal_volume

17

pub_type

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