Meta-analysis reveals materiomic relationships in major ampullate silk across the spider phylogeny

• Published in: Journal of the Royal Society interface 2020-09, Vol.17 (170), p.20200471-20200471
• Main Authors: Craig, Hamish C, Piorkowski, Dakota, Nakagawa, Shinichi, Kasumovic, Michael M, Blamires, Sean J
• Format: Article
• Language: English
• Subjects: Amino Acids; Animals; Fibroins - genetics; Life Sciences–Chemistry interface; Phylogeny; Silk - genetics; Spiders - genetics
• ISSN: 1742-5689; 1742-5662
• DOI: 10.1098/rsif.2020.0471

Spider major ampullate (MA) silk, with its combination of strength and extensibility, outperforms any synthetic equivalents. There is thus much interest in understanding its underlying materiome. While the expression of the different silk proteins (spidroins) appears an integral component of silk performance, our understanding of the nature of the relationship between the spidroins, their constituent amino acids and MA silk mechanics is ambiguous. To provide clarity on these relationships across spider species, we performed a meta-analysis using phylogenetic comparative methods. These showed that glycine and proline, both of which are indicators of differential spidroin expression, had effects on MA silk mechanics across the phylogeny. We also found serine to correlate with silk mechanics, probably via its presence within the carboxyl and amino-terminal domains of the spidroins. From our analyses, we concluded that the spidroin expression shifts across the phylogeny from predominantly MaSp1 in the MA silks of ancestral spiders to predominantly MaSp2 in the more derived spiders' silks. This trend was accompanied by an enhanced ultimate strain and decreased Young's modulus in the silks. Our meta-analysis enabled us to decipher between real and apparent influences on MA silk properties, providing significant insights into spider silk and web coevolution and enhancing our capacity to create spider silk-like materials.