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Structure/function analysis of spinalin, a spine protein of Hydra nematocysts

The nematocyst capsules of the cnidarians are specialized explosive organelles that withstand high osmotic pressures of ≈15 MPa (150 bar). A tight disulfide network involving cysteine-rich capsule wall proteins, like minicollagens and nematocyst outer wall antigen, characterizes their molecular comp...

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Main Authors: Hellstern, Simon (Author) , Holstein, Thomas W. (Author) , Özbek, Suat (Author)
Format: Article (Journal)
Language:English
Published: 15 June 2006
In: The FEBS journal
Year: 2006, Volume: 273, Issue: 14, Pages: 3230-3237
ISSN:1742-4658
DOI:10.1111/j.1742-4658.2006.05331.x
Online Access:Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1111/j.1742-4658.2006.05331.x
Verlag, kostenfrei, Volltext: http://onlinelibrary.wiley.com/doi/10.1111/j.1742-4658.2006.05331.x/abstract
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Author Notes:Simon Hellstern, Jörg Stetefeld, Charlotte Fauser, Ariel Lustig, Jürgen Engel, Thomas W. Holstein, Suat Özbek

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520 |a The nematocyst capsules of the cnidarians are specialized explosive organelles that withstand high osmotic pressures of ≈15 MPa (150 bar). A tight disulfide network involving cysteine-rich capsule wall proteins, like minicollagens and nematocyst outer wall antigen, characterizes their molecular composition. Nematocyst discharge leads to the expulsion of a long inverted tubule that was coiled inside the capsule matrix before activation. Spinalin has been characterized as a glycine-rich, histidine-rich protein associated with spine structures on the surface of everted tubules. Here, we show that full-length Hydra spinalin can be expressed recombinantly in HEK293 cells and has the property to form disulfide-linked oligomers, reflecting its state in mature capsules. Furthermore, spinalin showed a high tendency to associate into dimers in vitro and in vivo. Our data, which show incomplete disulfide connectivity in recombinant spinalin, suggest a possible mechanism by which the spine structure may be linked to the overall capsule polymer. 
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