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Comparative Proteomic Analysis of Hymenolepis diminuta Cysticercoid and Adult Stages.

Authors :
Sulima, Anna
Savijoki, Kirsi
Bień, Justyna
Näreaho, Anu
Sałamatin, Rusłan
Conn, David Bruce
Młocicki, Daniel
Source :
Frontiers in Microbiology; 1/15/2018, p1-N.PAG, 14p
Publication Year :
2018

Abstract

Cestodiases are common parasitic diseases of animals and humans. As cestodes have complex lifecycles, hexacanth larvae, metacestodes (including cysticercoids), and adults produce proteins allowing them to establish invasion and to survive in the hostile environment of the host. Hymenolepis diminuta is the most commonly used model cestode in experimental parasitology. The aims of the present study were to perform a comparative proteomic analysis of two consecutive developmental stages of H. diminuta (cysticercoid and adult) and to distinguish proteins which might be characteristic for each of the stages from those shared by both stages. Somatic proteins of H. diminuta were isolated from 6-week-old cysticercoids and adult tapeworms. Cysticercoids were obtained from experimentally infected beetles, Tenebrio molitor, whereas adult worms were collected from experimentally infected rats. Proteins were separated by GeLC-MS/MS (one dimensional gel electrophoresis coupled with liquid chromatography and tandem mass spectrometry). Additionally protein samples were digested in-liquid and identified by LC-MS/MS. The identified proteins were classified according to molecular function, cellular components and biological processes. Our study showed a number of differences and similarities in the protein profiles of cysticercoids and adults; 233 cysticercoid and 182 adult proteins were identified. From these proteins, 131 were present only in the cysticercoid and 80 only in the adult stage samples. Both developmental stages shared 102 proteins; among which six represented immunomodulators and one is a potential drug target. In-liquid digestion and LC-MS/MS complemented and confirmed some of the GeLC-MS/MS identifications. Possible roles and functions of proteins identified with both proteomic approaches are discussed. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
1664302X
Database :
Complementary Index
Journal :
Frontiers in Microbiology
Publication Type :
Academic Journal
Accession number :
127425395
Full Text :
https://doi.org/10.3389/fmicb.2017.02672