Giant wood spider Nephila pilipes alters silk protein in response to prey variation.
Recent studies have demonstrated that orb-weaving spiders may alter web structures, foraging localities or silk output in response to prey variations. In this study we conducted field surveys and food manipulations to examine whether orb-weaving spiders may also adjust the protein of silk to prey variations. A comparison of dragline silks collected from nine giant wood spider Nephila pilipes populations in Taiwan showed a spatial variation. The percentage of all amino acids (except alanine and glycine) exhibited significant differences among populations. A survey of prey composition also revealed a significant spatial variation among N. pilipes populations. To determine whether prey variation was responsible for silk protein variation, we fed N. pilipes with different types of prey (dipteran vs orthopteran) then compared the percentage of five major dragline amino acids and secondary structures. The results showed that dragline of N. pilipes fed with orthopteran prey contained significantly higher proline and glutamine but lower alanine. Congruent with this result were those from FTIR spectroscopy, which showed that dragline of N. pilipes fed with crickets exhibited significantly higher percentage of proline- and glutamine-containing beta turns, and lower percentage of alanine-containing beta sheet structures. Since the results of feeding manipulations showed that diet significantly affected the compositions of dragline silks, the observed spatial variation seemed to reflect the different types of prey these spiders had consumed. Results of this study thus indicated that orb-weaving spiders can alter dragline protein in response to prey variations.
Tso
I-Min
IM
Department of Life Sciences, Tunghai University, Taichung 407, Taiwan. spider@mail.thu.edu.tw
Wu
Hsuan-Chen
HC
Hwang
In-Ru
IR
D000596:Amino Acids / Q000032:analysis*; D000704:Analysis of Variance; D000818:Animals; D004032:Diet; D007313:Insecta; D011235:Predatory Behavior / Q000502:physiology*; D011487:Protein Conformation; D047011:Silk / Q000737:chemistry*; D017550:Spectroscopy, Fourier Transform Infrared; D013112:Spiders / Q000737:chemistry / Q000502:physiology*; D013624:Taiwan
D000596:Amino Acids; D047011:Silk