Environmental response and adaptation of glycoprotein glue within the droplets of viscous prey capture threads from araneoid spider orb-webs
Viscous threads that form the prey capture spiral of araneoid orb-webs retain insects that strike the web, giving a spider more time to locate and subdue them. The viscoelastic glycoprotein glue responsible for this adhesion forms the core of regularly spaced aqueous droplets, which are supported by protein axial fibers. Glycoprotein extensibility both facilitates the recruitment of adhesion from multiple droplets and dissipates the energy generated by insects struggling to free themselves from the web. Compounds in the aqueous material make the droplets hygroscopic, causing an increase in both droplet volume and extensibility as humidity ( RH) rises. We characterized these humidity-mediated responses at 20%, 37%, 55%, 72% and 90% RH in two large orbweavers, Argiope aurantia, which is found in exposed habitats, and Neoscona crucifera, which occupies forests and forest edges. The volume-specific extension of A. aurantia glycoprotein reached a maximum value at 55% RH and then declined, whereas that of N. crucifera increased exponentially through the RH range. As RH increased, the relative stress on droplet filaments at maximum extension, as gauged by axial line deflection, decreased in a linear fashion in A. aurantia, but in N. crucifer increased logarithmically, indicating that N. crucifera threads are better equipped to dissipate energy through droplet elongation. The greater hygroscopicity of A. aurantia threads equips them to function in lower RH environments and during the afternoon when RH drops, but their performance is diminished during the high RH of the morning hours. In contrast, the lower hygroscopicity of N. crucifera threads optimizes their performance for intermediate and high RH environments and during the night and morning. These interspecific differences support the hypothesis that viscous capture threads are adapted to the humidity regime of an orbweavers habitat.