Structural characterization and biological implications of sulfated N-glycans in a serine protease from the neotropical moth Hylesia metabus (Cramer [1775]) (Lepidoptera : Saturniidae). Article - Novembre 2015

Gleysin Cabrera, Víctor Salazar, Raquel Montesino, Yanet Támbara, Weston B Struwe, Evelyn Leon, David J Harvey, Antoine Lesur, Mónica Rincón, Bruno Domon, Milagros Méndez, Madelón Portela, Annia González, Ada Triguero, Rosario Durán, Ulf Lundberg, Eva Vonasek, Luis Javier González

Gleysin Cabrera, Víctor Salazar, Raquel Montesino, Yanet Támbara, Weston B Struwe, Evelyn Leon, David J Harvey, Antoine Lesur, Mónica Rincón, Bruno Domon, Milagros Méndez, Madelón Portela, Annia González, Ada Triguero, Rosario Durán, Ulf Lundberg, Eva Vonasek, Luis Javier González, « Structural characterization and biological implications of sulfated N-glycans in a serine protease from the neotropical moth Hylesia metabus (Cramer [1775]) (Lepidoptera : Saturniidae).  », Glycobiology, novembre 2015, pp. 230-250. ISSN 0959-6658

Abstract

Contact with the urticating setae from the abdomen of adult females of the neo-tropical moth Hylesia metabus gives rise to an urticating dermatitis, characterized by intense pruritus, generalized malaise and occasionally ocular lesions (lepidopterism). The setae contain a pro-inflammatory glycosylated protease homologous to other S1A serine proteases of insects. Deglycosylation with PNGase F in the presence of a buffer prepared with 40% H2 (18)O allowed the assignment of an N-glycosylation site. Five main paucimannosidic N-glycans were identified, three of which were exclusively α(1-6)-fucosylated at the proximal GlcNAc. A considerable portion of these N-glycans are anionic species sulfated on either the 4- or the 6-position of the α(1-6)-mannose residue of the core. The application of chemically and enzymatically modified variants of the toxin in an animal model in guinea pigs showed that the pro-inflammatory and immunological reactions, e.g. disseminated fibrin deposition and activation of neutrophils, are due to the presence of sulfate-linked groups and not on disulfide bonds, as demonstrated by the reduction and S-alkylation of the toxin. On the other hand, the hemorrhagic vascular lesions observed are attributed to the proteolytic activity of the toxin. Thus, N-glycan sulfation may constitute a defense mechanism against predators.

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