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

Gleysin Cabrera 1 Víctor Salazar 2 Raquel Montesino 3 Yanet Támbara 1 Weston B Struwe 4 Evelyn Leon 2 David J Harvey 5 Antoine Lesur 6 Mónica Rincón 2 Bruno Domon 6 Milagros Méndez 2 Madelón Portela 7 Annia González 1 Ada Triguero 1 Rosario Durán 7 Ulf Lundberg 2 Eva Vonasek 2 Luis Javier González 1
1 CIGB - Center for Genetic Engineering and Biotechnology [Cuba]
2 Venezuelan Institute for Scientific Research
3 Universidad de Concepción [Chile]
4 University of Oxford [Oxford]
5 Glycobiology Institute
6 Luxembourg Clinical Proteomics Center
7 Institut Pasteur de Montevideo
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.
Keywords : Hylesia metabus insects lepidopterism serine protease sulfated N-glycans
Type de document :
Article dans une revue
Glycobiology, Oxford University Press (OUP), 2015, pp.230-50
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Contributeur : Mariella Botta <>
Soumis le : mercredi 29 mars 2017 - 19:14:12
Dernière modification le : lundi 8 octobre 2018 - 17:44:06

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  • HAL Id : pasteur-01498327, version 1
  • PUBMED : 26537504

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Gleysin Cabrera, Víctor Salazar, Raquel Montesino, Yanet Támbara, Weston B Struwe, et al.. Structural characterization and biological implications of sulfated N-glycans in a serine protease from the neotropical moth Hylesia metabus (Cramer [1775]) (Lepidoptera: Saturniidae).. Glycobiology, Oxford University Press (OUP), 2015, pp.230-50. 〈pasteur-01498327〉

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