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Identification of immunogenic proteins of the cysticercoid of Hymenolepis diminuta.

Authors :
Sulima, Anna
Bień, Justyna
Savijoki, Kirsi
Näreaho, Anu
Sałamatin, Rusłan
Conn, David Bruce
Młocicki, Daniel
Source :
Parasites & Vectors; 11/21/2017, Vol. 10, p1-12, 12p
Publication Year :
2017

Abstract

Background: A wide range of molecules are used by tapeworm metacestodes to establish successful infection in the hostile environment of the host. Reports indicating the proteins in the cestode-host interactions are limited predominantly to taeniids, with no previous data available for non-taeniid species. A non-taeniid, Hymenolepis diminuta, represents one of the most important model species in cestode biology and exhibits an exceptional developmental plasticity in its life-cycle, which involves two phylogenetically distant hosts, arthropod and vertebrate. Results: We identified H. diminuta cysticercoid proteins that were recognized by sera of H. diminuta-infected rats using two-dimensional gel electrophoresis (2DE), 2D-immunoblotting, and LC-MS/MS mass spectrometry. Proteomic analysis of 42 antigenic spots revealed 70 proteins. The largest number belonged to structural proteins and to the heat-shock protein (HSP) family. These results show a number of the antigenic proteins of the cysticercoid stage, which were present already in the insect host prior to contact with the mammal host. These are the first parasite antigens that the mammal host encounters after the infection, therefore they may represent some of the molecules important in host-parasite interactions at the early stage of infection. Conclusions: These results could help in understanding how H. diminuta and other cestodes adapt to their diverse and complex parasitic life-cycles and show universal molecules used among diverse groups of cestodes to escape the host response to infection. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
17563305
Volume :
10
Database :
Complementary Index
Journal :
Parasites & Vectors
Publication Type :
Academic Journal
Accession number :
126351464
Full Text :
https://doi.org/10.1186/s13071-017-2519-4