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A lipid transfer protein ensures nematode cuticular impermeability

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Njume, Ferdinand Ngale | Razzauti, Adria | Soler, Miguel | Perschin, Veronika | Fazeli, Gholamreza | Bourez, Axelle | Delporte, Cedric | Ghogomu, Stephen | Poelvoorde, Philippe | Pichard, Simon | Birck, Catherine | Poterszman, Arnaud | Souopgui, Jacob | van Antwerpen, Pierre | Stigloher, Christian | Vanhamme, Luc | Laurent, Patrick

Edité par CCSD ; Elsevier -

International audience. The cuticle of C. elegans is impermeable to chemicals, toxins, and pathogens. However, increased permeability is a desirable phenotype because it facilitates chemical uptake. Surface lipids contribute to the permeability barrier. Here, we identify the lipid transfer protein GMAP-1 as a critical element setting the permeability of the C. elegans cuticle. A gmap-1 deletion mutant increases cuticular permeability to sodium azide, levamisole, Hoechst, and DiI. Expressing GMAP-1 in the hypodermis or transiently in the adults is sufficient to rescue this gmap-1 permeability phenotype. GMAP-1 protein is secreted from the hypodermis to the aqueous fluid filling the space between collagen fibers of the cuticle. In vitro, GMAP-1 protein binds phosphatidylserine and phosphatidylcholine while in vivo, GMAP-1 sets the surface lipid composition and organization. Altogether, our results suggest GMAP-1 secreted by hypodermis shuttles lipids to the surface to form the permeability barrier of C. elegans.

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