The Major Surface Carbohydrates of the <i>Echinococcus granulosus</i> Cyst: Mucin-Type <i>O</i>-Glycans Decorated by Novel Galactose-Based Structures

Díaz, Álvaro; Fontana, Carolina; Todeschini, Adriane R.; Soulé, Silvia; González, Humberto; Casaravilla, Cecilia; Portela, Magdalena; Mohana‐Borges, Ronaldo; Mendonça-Previato, Lúcia; Ferreira, Fernando

doi:10.1021/bi901112q

Cited by 35 publications

(16 citation statements)

References 49 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In TLC test, the strip of the LL Ag bands may indicate the presence of a wide range of different sugar in this layer, while PS Ag and CF Ag showed 2 bands or no band, respectively. In agreement with this result it has been shown that laminated layer is highly glycosylated ( 38 - 40 ).…”

Section: Discussionsupporting

confidence: 85%

Antibody response to glycan antigens of hydatid cyst fluid, laminated layer and protoscolex of Echinococcus granulosus

Rafiei-Sefiddashti

Sharafi

Ebrahimi

et al. 2017

Med J Islam Repub Iran

View full text Add to dashboard Cite

Background: Hydatid disease is characterized by long-term growth of hydatid cysts in the human. The glycan antigens have an important role in the immunology of hydatid cyst. In this study immunological reaction of host sera to different glycan antigens of the cyst, has been investigated. Methods: The antibody responses were tested to glycoprotein and glycolipid of the laminated layer (LL), cyst fluid (CF) and protoscolex (PS) antigens of E. Granulosus using ELISA and western immunoblotting tests. Thin-layer chromatography and ß-elimination were used for glycan purification. Results: Both hydatid cyst and normal human sera reacted with hydatid cyst fluid, protoscolices, laminated layer, glycoprotein and glycolipid antigens. The most antigen-antibody reaction was related to CF and PS antigens, and LL antigens had the minimal reaction with the sera. Thin layer chromatography (TLC) of the antigens showed presence of many glycan bands in the laminated layer. Conclusion: The parasite may elaborate different glycan antigens in LL to evade host immune response.

show abstract

Section: Discussionsupporting

confidence: 85%

Antibody response to glycan antigens of hydatid cyst fluid, laminated layer and protoscolex of Echinococcus granulosus

Rafiei-Sefiddashti

Sharafi

Ebrahimi

et al. 2017

Med J Islam Repub Iran

View full text Add to dashboard Cite

show abstract

“…Finally, in agreement with intense mucin biosynthesis, a number of CW clusters encode enzymes and transporters involved in the assembly of O -glycans ( Table 7 ). In particular, probably reflecting the marked predominance of galactose in the major glycans purified from the laminated layer [116], several transcripts correspond to proteins participating in galactose metabolism, the synthesis of UDP-galactose and its translocation across Golgi membranes.…”

Section: Resultsmentioning

confidence: 99%

A Transcriptomic Analysis of Echinococcus granulosus Larval Stages: Implications for Parasite Biology and Host Adaptation

et al. 2012

View full text Add to dashboard Cite

BackgroundThe cestode Echinococcus granulosus - the agent of cystic echinococcosis, a zoonosis affecting humans and domestic animals worldwide - is an excellent model for the study of host-parasite cross-talk that interfaces with two mammalian hosts. To develop the molecular analysis of these interactions, we carried out an EST survey of E. granulosus larval stages. We report the salient features of this study with a focus on genes reflecting physiological adaptations of different parasite stages.Methodology/Principal FindingsWe generated ∼10,000 ESTs from two sets of full-length enriched libraries (derived from oligo-capped and trans-spliced cDNAs) prepared with three parasite materials: hydatid cyst wall, larval worms (protoscoleces), and pepsin/H+-activated protoscoleces. The ESTs were clustered into 2700 distinct gene products. In the context of the biology of E. granulosus, our analyses reveal: (i) a diverse group of abundant long non-protein coding transcripts showing homology to a middle repetitive element (EgBRep) that could either be active molecular species or represent precursors of small RNAs (like piRNAs); (ii) an up-regulation of fermentative pathways in the tissue of the cyst wall; (iii) highly expressed thiol- and selenol-dependent antioxidant enzyme targets of thioredoxin glutathione reductase, the functional hub of redox metabolism in parasitic flatworms; (iv) candidate apomucins for the external layer of the tissue-dwelling hydatid cyst, a mucin-rich structure that is critical for survival in the intermediate host; (v) a set of tetraspanins, a protein family that appears to have expanded in the cestode lineage; and (vi) a set of platyhelminth-specific gene products that may offer targets for novel pan-platyhelminth drug development.Conclusions/SignificanceThis survey has greatly increased the quality and the quantity of the molecular information on E. granulosus and constitutes a valuable resource for gene prediction on the parasite genome and for further genomic and proteomic analyses focused on cestodes and platyhelminths.

show abstract

“…Certain of these N-terminal extensions bear unpaired cysteine residues, coincident with evidence that disulfide bonds contribute to the LL structure (7). The LL mucin glycans are now largely defined (13, 14). …”

Section: Introductionmentioning

confidence: 99%

Unconventional Maturation of Dendritic Cells Induced by Particles from the Laminated Layer of Larval Echinococcus granulosus

et al. 2014

Self Cite

View full text Add to dashboard Cite

The larval stage of the cestode parasite Echinococcus granulosus causes hydatid disease in humans and livestock. This infection is characterized by the growth in internal organ parenchymae of fluid-filled structures (hydatids) that elicit surprisingly little inflammation in spite of their massive size and persistence. Hydatids are protected by a millimeter-thick layer of mucin-based extracellular matrix, termed the laminated layer (LL), which is thought to be a major factor determining the host response to the infection. Host cells can interact both with the LL surface and with materials that are shed from it to allow parasite growth. In this work, we analyzed the response of dendritic cells (DCs) to microscopic pieces of the native mucin-based gel of the LL (pLL). In vitro, this material induced an unusual activation state characterized by upregulation of CD86 without concomitant upregulation of CD40 or secretion of cytokines (interleukin 12 [IL-12], IL-10, tumor necrosis factor alpha [TNF-α], and IL-6). When added to Toll-like receptor (TLR) agonists, pLL-potentiated CD86 upregulation and IL-10 secretion while inhibiting CD40 upregulation and IL-12 secretion. In vivo, pLL also caused upregulation of CD86 and inhibited CD40 upregulation in DCs. Contrary to expectations, oxidation of the mucin glycans in pLL with periodate did not abrogate the effects on cells. Reduction of disulfide bonds, which are known to be important for LL structure, strongly diminished the impact of pLL on DCs without altering the particulate nature of the material. In summary, DCs respond to the LL mucin meshwork with a “semimature” activation phenotype, both in vitro and in vivo.

show abstract

The Major Surface Carbohydrates of the Echinococcus granulosus Cyst: Mucin-Type O-Glycans Decorated by Novel Galactose-Based Structures

Cited by 35 publications

References 49 publications

Antibody response to glycan antigens of hydatid cyst fluid, laminated layer and protoscolex of Echinococcus granulosus

Antibody response to glycan antigens of hydatid cyst fluid, laminated layer and protoscolex of Echinococcus granulosus

A Transcriptomic Analysis of Echinococcus granulosus Larval Stages: Implications for Parasite Biology and Host Adaptation

Unconventional Maturation of Dendritic Cells Induced by Particles from the Laminated Layer of Larval Echinococcus granulosus

Contact Info

Product

Resources

About