Peroxinectin catalyzed dityrosine crosslinking in the adhesive underwater silk of a casemaker caddisfly larvae, Hysperophylax occidentalis

Ching Shuen Wang, Nicholas N. Ashton, Robert B. Weiss, Russell J. Stewart

研究成果: 雜誌貢獻文章同行評審

36 引文 斯高帕斯(Scopus)

摘要

Aquatic caddisfly larvae use sticky silk fibers as an adhesive tape to construct protective composite structures under water. Three new silk fiber components were identified by transcriptome and proteome analysis of the silk gland: a heme-peroxidase in the peroxinectin (Pxt) sub-family, a superoxide dismutase 3 (SOD3) that generates the H2O2 substrate of the silk fiber Pxt from environmental reactive oxygen species (eROS), and a novel structural component with sequence similarity to the elastic PEVK region of the muscle protein, titin. All three proteins are co-drawn with fibroins to form silk fibers. The Pxt and SOD3 enzymes retain activity in drawn fibers. In native fibers, Pxt activity and dityrosine crosslinks are co-localized at the boundary of a peripheral layer and the silk fiber core. To our knowledge, dityrosine crosslinks, heme peroxidase, and SOD3 activities have not been previously reported in an insect silk. The PEVK-like protein is homogeneously distributed throughout the fiber core. The results are consolidated into a model in which caddisfly silk Pxt-catalyzed dityrosine crosslinking occurs post-draw using H2O2 generated within the silk fibers by SOD3. The ROS substrate of caddisfly silk SOD3 occurs naturally in aquatic environments, from biotic and abiotic sources. The radially inhomogeneous dityrosine crosslinking and a potential titin-like PEVK protein network have important implications for the mechanical properties of caddifly silk fibers.
原文英語
頁(從 - 到)69-79
頁數11
期刊Insect Biochemistry and Molecular Biology
54
DOIs
出版狀態已發佈 - 11月 1 2014

ASJC Scopus subject areas

  • 生物化學
  • 分子生物學
  • 昆蟲科學

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