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Abstract

Mutations in the rtv gene cause disarrangement of chitin fibers in the cuticle of the Drosophila larva, and occasionally the cuticle detaches from the epidermis. We have identified the rtv gene, and using the new HHpred homology detection method, we show that the Rtv protein defines a new family of disulfide-rich proteins in insects that are related to vertebrate snake neurotoxin-like proteins, including CD59 and transforming growth factor-β type II receptors. Rtv is an extracellular membrane-anchored protein exposing six aromatic residues that may mediate binding to chitin. We propose that this binding function of Rtv may assist the organization of chitin fibers at the epidermal cell surface during cuticle assembly.