Unraveling the mechanical properties of composite silk threads spun by cribellate orb-weaving spiders.
Orb-web weaving spiders depend upon the mechanical performance of capture threads to absorb the energy of flying prey. Most orb-weavers spin wet capture threads with core fibers of flagelliform silk. These threads are extremely compliant and extensible due to the folding of their constituent proteins into molecular nanosprings and hydration by a surrounding coating of aqueous glue. In contrast, other orb-weavers use cribellate capture threads, which are composite structures consisting of core fibers of pseudoflagelliform silk surrounded by a matrix of fine dry cribellar fibrils. Based on phylogenetic evidence, cribellate capture threads predate the use of viscid capture threads. To better characterize how pseudoflagelliform and cribellar fibrils function, we investigated the mechanical performance of cribellate capture threads for three genera of spiders (Deinopis, Hyptiotes and Uloborus). These taxa spin very diverse web architectures, ranging from complete orbs to evolutionarily reduced triangle webs and cast nets. We found that the pseudoflagelliform core fibers of these webs were stiffer and stronger, but also less extensible, than flagelliform silk. However, cribellate capture threads achieved overall high extensibilities because the surrounding cribellar fibrils contributed substantially to the tensile performance of threads long after the core pseudoflagelliform fibers ruptured. In the case of Deinopis capture threads, up to 90% of the total work performed could be attributed to these fibrils. These findings yield insight into the evolutionary transition from cribellate to viscid capture threads.
Blackledge
Todd A
TA
Department of Biology, University of Akron, Akron, OH 44325-3908, USA. blackledge@uakron.edu
Hayashi
Cheryl Y
CY
D000818:Animals; D060829:Arthropod Proteins / Q000032:analysis / Q000737:chemistry* / Q000502:physiology; D005075:Biological Evolution; D001696:Biomechanical Phenomena; D004548:Elasticity; D019476:Insect Proteins / Q000032:analysis / Q000737:chemistry* / Q000502:physiology; D010802:Phylogeny; D011235:Predatory Behavior; D017510:Protein Folding; D047011:Silk / Q000032:analysis / Q000737:chemistry* / Q000502:physiology; D013112:Spiders / Q000145:classification / Q000378:metabolism / Q000502:physiology*
D060829:Arthropod Proteins; D019476:Insect Proteins; D047011:Silk