Identification of a laminated layer-associated protein in Echinococcus multilocularis metacestodes
| Autor: | Andrew Hemphill, Katrin Ingold, Bruno Gottstein |
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| Rok vydání: | 1998 |
| Předmět: |
Octoxynol
Cestoda Antibodies Helminth Antibody Affinity Echinococcus multilocularis Host-Parasite Interactions Polyethylene Glycols Microbiology Mice Echinococcosis medicine Animals Parasite hosting Fluorescent Antibody Technique Indirect Antiserum biology 630 Agriculture Helminth Proteins Viral tegument biology.organism_classification medicine.disease Immunohistochemistry Echinococcus Mice Inbred C57BL Metacestode Infectious Diseases Antigens Helminth Larva Immunology Animal Science and Zoology Parasitology |
| Zdroj: | Ingold, K; Gottstein, Bruno; Hemphill, A (1998). Identification of a laminated layer-associated protein in Echinococcus multilocularis metacestodes. Parasitology, 116(04), pp. 363-372. Cambridge University Press 10.1017/S0031182098002406 |
| DOI: | 10.48350/118734 |
| Popis: | Echinococcus multilocularis is a cestode parasite that predominantly infects red and arctic foxes as definitive hosts. Ingestion of E. multilocularis eggs and subsequent post-oncospheral infection with the larval stage (metacestode) of the parasite results in alveolar echinococcosis (AE), a life-threatening hepatic disease concerning humans and other intermediate hosts such as small rodents. The primary fluid-filled vesicles of the asexually proliferating metacestode are comprised of an inner germinal layer, a syncytial tegument, and an outer, acellular, so-called laminated layer. This laminated layer may play an important role in protecting the developing E. multilocularis metacestode from host immune reactions, and laminated layer-associated components represent potential targets for intervention during the course of AE. We have used an in vitro cultivation technique for the long-term maintenance and proliferation of E. multilocularis metacestodes in order to generate premature (protoscolex-free) parasite vesicles. A polyclonal antiserum was raised against this host-free parasite tissue. Subsequent immunoblot analysis of parasite fractions obtained by Triton X-114 extraction led to the identification of a 116 kDa protein (named EmP2) within the Triton-insoluble fraction. The characterization of EmP2 by SDS–PAGE, Western blotting, and by immunofluorescence revealed that EmP2 is a laminated layer-associated protein. |
| Databáze: | OpenAIRE |
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