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 Repjournal_title
EMBO reportsauthors
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 CZdoi
10.15252/embr.201540851subject
Has Abstractpub_date
2016-02-01 00:00:00pages
235-48issue
2eissn
1469-221Xissn
1469-3178pii
embr.201540851journal_volume
17pub_type
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