A cysteine‐rich protein in the <i>Theromyzon</i> (Annelida: Hirudinea) cocoon membrane

Abstract

The aquatic leech, Theromyzon rude, secretes a flexible, proteinaceous cocoon that is resistant to a broad range of denaturing conditions (e.g. heat, denaturing chemicals). We have partially solubilized the Theromyzon cocoon membrane in 10% acetic acid and identified two major protein fragments. Microsequencing of both Theromyzon cocoon protein (Tcp) fragments generated an identical stretch of the amino-terminal sequence that was used to clone the corresponding gene. The predicted linear amino acid sequence of the resulting cDNA contained an unusually high cysteine content (17.8%). Sequence analysis identified six internal repeats, each comprising 12 ordered Cys residues in a approximately 62 amino acid repeating unit. Sequence comparisons identified homology with undescribed, Cys-rich repeats across animal phyla (i.e. Arthropod, Nematoda).