A 78 kDa glucose-regulated protein gene of<i>Spirometra erinacei</i>plerocercoid induced by chemical and physiological stresses

Yun, Doo-Hee; Bae, Young-An; Chung, Joon‐Yong; Kang, Sung-Soo; Kang, In‐Cheol; Sohn, Woon-Mok; Cho, S.-H.; Kim, T.-S.; Cho, S.-Y.; Kong, Yoon

doi:10.1017/s0031182004006158

Cited by 2 publications

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“…It has been found that this protein is an immunodominant antigen in echinococcal disease [ 51 ]. The results of research by Yun et al [ 52 ] suggest that GRP78 functions as a molecular chaperone in adapting parasites to the new host environment. Whereas apolipoprotein A-I is the major apolipoprotein of high density lipoproteins (HDL) and has an important role in the regulation of the lipid transport, stability, structure, and metabolism of HDL particles [ 53 ].…”

Section: Discussionmentioning

confidence: 99%

Identification of immunogenic proteins of the cysticercoid of Hymenolepis diminuta

et al. 2017

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BackgroundA 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.ResultsWe 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.ConclusionsThese 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.Electronic supplementary materialThe online version of this article (10.1186/s13071-017-2519-4) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

Identification of immunogenic proteins of the cysticercoid of Hymenolepis diminuta

et al. 2017

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“…GRP78 is an immunoglobulin heavy chain binding protein and a member of hsp70 protein family (Munro and Pelham, 1986 ). Yun et al ( 2004 ) suggest that GRP78 functions as a molecular chaperone in adapting parasites to the new host environment. In E. granulosus and E. multilocularis infections, EM-GRP78 ( E. multilocularis GRP78) is an immunodominant antigen (Mühlschlegel et al, 1995 ).…”

Section: Discussionmentioning

confidence: 99%

Comparative Proteomic Analysis of Hymenolepis diminuta Cysticercoid and Adult Stages

et al. 2018

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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.

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A 78 kDa glucose-regulated protein gene ofSpirometra erinaceiplerocercoid induced by chemical and physiological stresses

Cited by 2 publications

References 32 publications

Identification of immunogenic proteins of the cysticercoid of Hymenolepis diminuta

Identification of immunogenic proteins of the cysticercoid of Hymenolepis diminuta

Comparative Proteomic Analysis of Hymenolepis diminuta Cysticercoid and Adult Stages

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