Abstract
Orb-weaving spiders spin a mechanically and functionally diverse range of silk fibers, each composed of one or more specific silk proteins. Of all silk types, wrapping silk combines high strength and extensibility and is made of multiple aciniform silk proteins (AcSp) that can be grouped into two AcSp types (AcSp1 and AcSp2) according to their distinct repetitive regions. Here, we present a novel and complete AcSp gene from orb weaving spider Araneus ventricosus. Phylogenetic analysis of the terminal regions of spidroins reveals that the new silk protein and the published A. ventricosus AcSp2 together form a subclade, indicating that this protein is a member of AcSp2 subclass and therefore named AcSp2 variant 2 (AcSp2-v2). The repetitive region of A. ventricosus AcSp2-v2 contains 24 cysteine residues, which is the first time that cysteine has been found in repetitive regions of spidroins. Moreover, the discovery of the ability of AcSp2-v2 repetitive domain to self-assemble into silk fibers expands the repertoire of known self-assembling sequences.
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