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J Exp Biol. 2014 May 1;217(Pt 9):1563-9. doi: 10.1242/jeb.097816. Epub 2014 Feb 5.

Temperature mediates the effect of humidity on the viscoelasticity of glycoprotein glue within the droplets of an orb-weaving spider's prey capture threads.

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Department of Biological Sciences, Virginia Tech, Blacksburg, VA 24061, USA.


Sticky viscous prey capture threads retain insects that strike araneoid orb-webs. The threads' two axial fibers support a series of glue droplets, each featuring a core of adhesive viscoelastic glycoprotein covered by an aqueous solution. After sticking, the glue extends, summing the adhesion of multiple droplets, and dissipates some of the energy of a struggling prey. As a day progresses, threads experience a drop in humidity and an increase in temperature, environmental variables that have the potential to alter thread and web function. We hypothesize that thread droplets respond to these opposing environmental changes in a manner that stabilizes their performance, and test this by examining threads spun by Argiope aurantia, a species that occupies exposed, weedy habitats. We confirmed that decreased humidity increases glycoprotein viscosity and found that increased temperature had the opposite effect. To evaluate the combined effect of temperature and humidity on a droplet's ability to transfer adhesive force and dissipate energy, we extended a droplet and measured both the deflection of the axial line supporting the droplet and the duration of its tensive load. The cumulative product of these two indices, which reflects the energy required to extend a droplet, was greatest under afternoon (hot and dry) conditions, less under morning (cool and humid) conditions, and least under hot and humid afternoon conditions. Although the opposing effects of temperature and humidity tend to stabilize glycoprotein performance, A. aurantia thread droplets appear to function optimally during the afternoon, equipping this species to capture large orthopterans, which are most active at this time.


Argiope aurantia; Biomaterial; Glycoprotein; Hygroscopic; Viscoelastic

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