First diagnosis of an imported human myiasis caused by Hypoderma sinense (Diptera: Oestridae), detected in a European traveler returning from India

This paper reports a case of myiasis caused by Hypoderma sinense in a European man returning from a journey through northern India. The patient showed eosinophilia, systemic signs of inflammation, and painful swellings in several parts of the body. The diagnosis was confirmed by specific serology and parasite molecular identification

The time course of biological and immunochemical allergy states induced by anisakis simplex larvae in rats

Oral infection by Anisakis simplex third stage larvae (L3) frequently gives rise to an allergic response. To comprehend the allergic and immune responses induced by L3, we investigated the kinetics of specific antibody isotype expression and the time course of biological and immunochemical allergy states using sera prepared from rats orally infected with L3 twice, with an interval of 9 weeks between infections. Biological and immunochemical allergy states were analysed by RBL-2H3 exocytosis and by indirect ELISA for IgE, respectively. The peak IgM at reinfection (RI) was comparable or similar to that at primary infection (PI) both in levels analysed by indirect ELISA and in antigen recognition analysed by Western blot. IgG1 and IgG2a levels were higher and showed accelerated kinetics after RI vs. after PI. However, the level of IgG2b was substantially lower than that of IgG2a. Peak immunochemical and biological allergy states for RI were higher and were reached faster than those for PI. The peak biological allergy state was observed at 1 week postreinfection and this occurred sooner than that for the peak immunochemical allergy state found at 2 weeks postreinfection. Our analysis of the relationship between specific IgE avidity and biological allergy state did not show any meaningful correlation. These results suggest that the allergic response induced by L3 oral infection is predominantly caused by reinfection and that this is accompanied by an elevated IgM level, which further suggests that the biological allergy state might not be related to specific IgE avidity

Human DNA-Damage-Inducible 2 Protein Is Structurally and Functionally Distinct from Its Yeast Ortholog

Although Ddi1-like proteins are conserved among eukaryotes, their biological functions remain poorly characterized. Yeast Ddi1 has been implicated in cell cycle regulation, DNA-damage response, and exocytosis. By virtue of its ubiquitin-like (UBL) and ubiquitin-associated (UBA) domains, it has been proposed to serve as a proteasomal shuttle factor. All Ddi1-like family members also contain a highly conserved retroviral protease-like (RVP) domain with unknown substrate specificity. While the structure and biological function of yeast Ddi1 have been investigated, no such analysis is available for the human homologs. To address this, we solved the 3D structures of the human Ddi2 UBL and RVP domains and identified a new helical domain that extends on either side of the RVP dimer. While Ddi1-like proteins from all vertebrates lack a UBA domain, we identify a novel ubiquitin-interacting motif (UIM) located at the C-terminus of the protein. The UIM showed a weak yet specific affinity towards ubiquitin, as did the Ddi2 UBL domain. However, the full-length Ddi2 protein is unable to bind to di-ubiquitin chains. While proteomic analysis revealed no activity, implying that the protease requires other factors for activation, our structural characterization of all domains of human Ddi2 sets the stage for further characterization