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Crustacean larval factor shares structural characteristics with the insect-specific follicle cell protein
Journal article   Open access   Peer reviewed

Crustacean larval factor shares structural characteristics with the insect-specific follicle cell protein

Tomer Ventura, Chan D H Nguyen, Quinn P Fitzgibbon, Tomer Abramov, Gregory G Smith and Abigail Elizur
Scientific Reports, Vol.9, 2847
2019
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Published VersionCC BY V4.0 Open Access
url
https://doi.org/10.1038/s41598-019-39173-7View
Published Version

Abstract

Literature on the cuticle formation in larval stages of the diverse group of decapod crustaceans is lacking, as opposed to a wealth of knowledge in several insect groups. Here we provide the first glimpse of the cuticular organisation in larvae of the eastern spiny lobster Sagmariasus verreauxi. A bioinformatic approach applied to S. verreauxi transcriptome through metamorphosis identified for the first time a small secreted protein with multiple isoforms that is highly expressed in crustacean larvae. This protein, named crustacean larval factor (Clf) shares structural characteristics with insect follicle cell protein 3 (FCP3), an insect-specific, rapidly evolving protein, with spatial-temporal regulated expression that is restricted to follicular cells during the production of the vitellin coat. Furthermore, we identified the FCP3 domain in additional structural proteins in multiple arthropod groups. Recombinant Clf inhibited in vitro calcium carbonate crystalline precipitation, in keeping with the finding that the spiny lobster larval cuticle is mainly composed of amorphous calcium carbonate. In addition, the recombinant Clf was shown to bind chitosan. Taken together, this research identifies two novel structural domains with lineage-specific expansion across arthropods. In crustaceans, Clf is found predominantly in larvae and the spatial-temporal regulated FCP3 factor occurs as a domain identified in multiple structural proteins across arthropods. Given the shared ten cysteines backbone between the Clf and FCP domains, a shared evolution is suggested and should be further explored.

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Biochemistry & Molecular Biology

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