Silk from crickets: A new twist on spinning

Walker, Andrew A., Weisman, Sarah, Church, Jeffrey S., Merritt, David J., Mudie, Stephen T. and Sutherland, Tara D. (2012) Silk from crickets: A new twist on spinning. Plos One, 7 2: e30408-1-e30408-8. doi:10.1371/journal.pone.0030408


Author Walker, Andrew A.
Weisman, Sarah
Church, Jeffrey S.
Merritt, David J.
Mudie, Stephen T.
Sutherland, Tara D.
Title Silk from crickets: A new twist on spinning
Journal name Plos One   Check publisher's open access policy
ISSN 1932-6203
Publication date 2012-02
Sub-type Article (original research)
DOI 10.1371/journal.pone.0030408
Open Access Status DOI
Volume 7
Issue 2
Start page e30408-1
End page e30408-8
Total pages 8
Place of publication San Francisco, CA, United States
Publisher Public Library of Science
Collection year 2013
Language eng
Abstract Raspy crickets (Orthoptera: Gryllacrididae) are unique among the orthopterans in producing silk, which is used to build shelters. This work studied the material composition and the fabrication of cricket silk for the first time. We examined silk-webs produced in captivity, which comprised cylindrical fibers and flat films. Spectra obtained from micro-Raman experiments indicated that the silk is composed of protein, primarily in a beta-sheet conformation, and that fibers and films are almost identical in terms of amino acid composition and secondary structure. The primary sequences of four silk proteins were identified through a mass spectrometry/cDNA library approach. The most abundant silk protein was large in size (300 and 220 kDa variants), rich in alanine, glycine and serine, and contained repetitive sequence motifs; these are features which are shared with several known beta-sheet forming silk proteins. Convergent evolution at the molecular level contrasts with development by crickets of a novel mechanism for silk fabrication. After secretion of cricket silk proteins by the labial glands they are fabricated into mature silk by the labium-hypopharynx, which is modified to allow the controlled formation of either fibers or films. Protein folding into beta-sheet structure during silk fabrication is not driven by shear forces, as is reported for other silks.
Keyword Gryllacridids Orthoptera
Insect
Fibroin
Nest
Mori
Ultrastructure
Recognition
Spinneret
Proteins
Spiders
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes Article number e30408, Published: 15 February 2012.

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2013 Collection
School of Biological Sciences Publications
 
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