Structural characterization and biological implications of sulfat | 9593
Journal of Glycobiology

Journal of Glycobiology
Open Access

ISSN: 2168-958X

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

3rd Glycobiology World Congress

June 26-28, 2017 London, UK

Gleysin Cabrera, Victor Salazar, Raquel Montesino, Yanet T�?¡mbara, Weston B Struwe, Evelyn Leon, David J Harvey, Antoine Lesur, M�?³nica Rincon, Bruno Domon, Milagros Mendez, Madelon Portela, Annia Gonzalez-Hern�?¡ndez, Ada Triguero, Rosario Duran, Ulf Lundberg, Eva Vonasek and Luis Javier Gon

Center for Genetic Engineering and Biotechnology, Cuba
Venezuelan Institute for Scientific Research, Venezuela
Universidad de Concepci�?³n, Chile
University of Oxford, UK
Luxembourg Clinical Proteomics Center, Luxembourg
Unidad de Bioqu�?­mica y Prote�?³mica Anal�?­ticas, Uruguay

Posters & Accepted Abstracts: J Glycobiol

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 18O allowed the assignment of an N-glycosylation site. Five main paucimannosidic N-glycans were identified, three of which were exclusively �?±(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 �?±(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.

Biography :