title: Protein content of the Hylesia metabus egg nest setae (Cramer [1775]) (Lepidoptera: Saturniidae) and its association with the parental investment for the reproductive success and lepidopterism.
abstract: Hylesia metabus is a neotropical moth possessing toxic setae, which once in contact with the skin cause a severe dermatitis to humans known as lepidopterism. The only known function of the setae in the life cycle is to provide protection during the mating and egg-hatching stages. Approximately 65% of the protein content of the setae is a cluster of five proteases (28-45kDa) showing sequence homology to other S1A serine proteases. The N-glycans of a 40kDa protease are a mixture of neutral and sulfated G0F structures. The sulfated N-glycans have an important role in triggering the inflammatory response typical of lepidopterism while the proteolytic activity may promote the erosion of blood vessels and tissues causing focal hemorrhages. The presence of Chitinase and a 30kDa lipoprotein is probably related to the antifungal defense. In addition, chitin digestion of the setae may potentiate the inflammatory reaction caused by the toxins due to the formation of chitin adjuvants fragments. The combined effect of proteases and a chitinase may dissuade predating arthropods, by damaging their exoskeletons. Vitellogenin, a bacteriostatic protein, is able to recognize pathogen-associated patterns, which suggests its possible role in protecting the embryonated eggs from pathogenic microorganisms.
  
  
  
  The present study is the first report describing the different protein species present in the urticating egg nest setae of the neotropical moth Hylesia metabus - the most harmful of the Hylesia moths - causing a severe urticating dermatitis in humans known as lepidopterism. A distinctive feature of the venom is the presence of five different S1A serine proteases probably used to guarantee a more efficient degradation of a wider number of protein substrates. This work confirms that the presence of sulfated N-glycans is not an isolated finding since its presence has been demonstrated in two different proteases affirming that this PTM is of importance for the activation of the inflammatory response typical of lepidopterism. Additionally, this study gives useful information on the defense mechanisms used for protection of its progeny vs. vertebrate predators, fungus, bacteria or other arthropods such as ants. The proteins detected in the egg nest should be seen as an extended parental effort made by the females in order to achieve an optimal reproductive success, thus compensating for the considerable loss of progeny during the larval stages that seriously limits the number of sexually mature adults reaching the reproductive phase.
authors: Mass Spectrometry Laboratory and GlycoLab, Department of Proteomics, Center for Genetic Engineering and Biotechnology, PO Box 6162, Havana, Cuba.
authors: Gleysin
authors: G
authors: Cabrera
authors: Unit for Invertebrate Toxins, Venezuelan Institute for Scientific Research, PO Box 20632, Caracas 1020A, Venezuela.
authors: Ulf
authors: U
authors: Lundberg
authors: Mass Spectrometry Laboratory and GlycoLab, Department of Proteomics, Center for Genetic Engineering and Biotechnology, PO Box 6162, Havana, Cuba.
authors: Arielis
authors: A
authors: Rodríguez-Ulloa
authors: Coordinación de Vigilancia Entomológica, Gerencia de Saneamiento Ambiental y Control de Endemias, FUNDASALUD, Carúpano, Estado Sucre, Venezuela.
authors: Melfran
authors: M
authors: Herrera
authors: Mass Spectrometry Laboratory and GlycoLab, Department of Proteomics, Center for Genetic Engineering and Biotechnology, PO Box 6162, Havana, Cuba.
authors: Wendy
authors: W
authors: Machado
authors: IIBCE y Unidad de Bioquímica y Proteómica Analíticas, Institut Pasteur de Montevideo, Mataojo 2020, Montevideo, Uruguay.
authors: Madelón
authors: M
authors: Portela
authors: Bioinformatic Department, Center for Genetic Engineering and Biotechnology, PO Box 6162, Havana, Cuba.
authors: Sucel
authors: S
authors: Palomares
authors: Mass Spectrometry Laboratory and GlycoLab, Department of Proteomics, Center for Genetic Engineering and Biotechnology, PO Box 6162, Havana, Cuba.
authors: Luis Ariel
authors: LA
authors: Espinosa
authors: Mass Spectrometry Laboratory and GlycoLab, Department of Proteomics, Center for Genetic Engineering and Biotechnology, PO Box 6162, Havana, Cuba.
authors: Yassel
authors: Y
authors: Ramos
authors: IIBCE y Unidad de Bioquímica y Proteómica Analíticas, Institut Pasteur de Montevideo, Mataojo 2020, Montevideo, Uruguay.
authors: Rosario
authors: R
authors: Durán
authors: Mass Spectrometry Laboratory and GlycoLab, Department of Proteomics, Center for Genetic Engineering and Biotechnology, PO Box 6162, Havana, Cuba.
authors: Vladimir
authors: V
authors: Besada
authors: Proteomics Unit, Center of Structural Biology, Venezuelan Institute for Scientific Research, PO Box 20632, Caracas 1020A, Venezuela.
authors: Eva
authors: E
authors: Vonasek
authors: Mass Spectrometry Laboratory and GlycoLab, Department of Proteomics, Center for Genetic Engineering and Biotechnology, PO Box 6162, Havana, Cuba. Electronic address: luis.javier@cigb.edu.cu.
authors: Luis Javier
authors: LJ
authors: González
mesh_terms: D000818:Animals; D003872:Dermatitis / Q000378:metabolism*; D005260:Female; D006801:Humans; D007249:Inflammation / Q000378:metabolism; D019476:Insect Proteins / Q000032:analysis* / Q000276:immunology / Q000378:metabolism; D009036:Moths / Q000378:metabolism* / Q000502:physiology; D009425:Nesting Behavior; D012098:Reproduction / Q000502:physiology; D058618:Sensilla / Q000737:chemistry / Q000378:metabolism*; D012726:Sexual Behavior, Animal; D015053:Zygote / Q000378:metabolism*
chemical_list: D019476:Insect Proteins
keywords: Chitinase; Hylesia metabus; Lepidopterism; Protease; Sulfated N-glycans; Vitellogenin