Novel assembly properties of recombinant spider dragline silk proteins

Daniel Huemmerich, Thomas Scheibel*, Fritz Vollrath, Shulamit Cohen, Uri Gat, Shmulik Ittah

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

159 Scopus citations

Abstract

Spider dragline silk, which exhibits extraordinary strength and toughness, is primarily composed of two related proteins that largely consist of repetitive sequences. In most spiders, the repetitive region of one of these proteins is rich in prolines, which are not present in the repetitive region of the other [1]. The absence of prolines in one component was previously speculated to be essential for the thread structure [2]. Here, we analyzed dragline proteins of the garden spider Araneus diadematus, ADF-3 and ADF-4, which are both proline rich, by employing the baculovirus expression system. Whereas ADF-3 represented an intrinsically soluble protein, ADF-4 was insoluble in vitro and self-assembled into filaments in the cytosol of the host insect cells. These ADF-4 filaments displayed the exceptional chemical stability of authentic silk threads. We provide evidence that the observed properties of ADF-3 and ADF-4 strongly depend on intrinsic characteristics such as hydropathicity, which differs dramatically between the two proteins, as in most other pairs of dragline silk proteins from other Araneoidea species, but not on their proline content. Our findings shed new light on the structural components of spider dragline silk, allowing further elucidation of their assembly properties, which may open the door for commercial applications.

Original languageAmerican English
Pages (from-to)2070-2074
Number of pages5
JournalCurrent Biology
Volume14
Issue number22
DOIs
StatePublished - 23 Nov 2004

Bibliographical note

Funding Information:
We thank John Gosline and Paul Guerette for kindly providing clones of adf-3 and adf-4, Bettina Richter for technical assistance, and Alexander Sponner and Michael Wise for critical comments on the manuscript. Special thanks to Naomi Melamed-Book for confocal microscopy/imaging and to Dr. Tsafi Danieli for help with baculovirus techniques. This work was supported by the Bundesministerium für Bildung und Forschung (D.H.), Fonds der Chemischen Industrie (D.H. and T.S.), and the Deutsche Forschungsgemeinschaft (T.S.).

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