Recent advances in characterization of Echinococcus antigen B

Mamuti, Wulamu; Sako, Yasuhito; Nakao, Minoru; Xiao, Ning; Nakaya, Kazuhiro; Ishikawa, Yuji; Yamasaki, Hiroshi; Lightowlers, Marshall W.; Itō, Akira

doi:10.1016/j.parint.2005.11.008

Cited by 52 publications

(41 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…4), indicating that EmABP is secreted by the E. multilocularis metacestode. For a control, we performed immunoprecipitation with an antibody against antigen B, one of the most abundant proteins in hydatid fluid (33). However, we never obtained bands despite the fact that antigen B was easily detected in hydatid fluid using the same antibody.…”

Section: Vol 77 2009 Echinococcus Apolipoprotein A-i Binding Proteimentioning

confidence: 96%

Molecular Characterization of EmABP, an Apolipoprotein A-I Binding Protein Secreted by the Echinococcus multilocularis Metacestode

Bernthaler

Epping

Schmitz³

et al. 2009

Infect Immun

View full text Add to dashboard Cite

Cestodes are unable to synthesize de novo most of their own membrane lipids, including cholesterol, and have to take them up from the host during an infection. The underlying molecular mechanisms are so far unknown. Here we report the identification and characterization of a novel gene, Emabp, which is expressed by larval stages and adults of the fox tapeworm Echinococcus multilocularis. The encoded protein, EmABP, displays significant homologies to apolipoprotein A-I binding protein (AI-BP) of mammalian origin and to metazoan YjeF_N domain proteins. Like mammalian AI-BP, EmABP carries an export-directing signal sequence which is absent in predicted AI-BP orthologs from the related flatworms Schistosoma japonicum and Schmidtea mediterranea. Using a specific antibody and immunoprecipitation techniques, we demonstrate that EmABP is secreted into the extraparasitic environment and into the hydatid fluid of in vitro-cultivated metacestode vesicles. Furthermore, we show that apolipoprotein A-I (apoA-I), a major constituent of cholesterol-transporting high-density lipoproteins, is present in hydatid fluid. By pulldown experiments, we demonstrate that recombinantly expressed, purified EmABP interacts with purified human apoA-I and is able to precipitate apoA-I from human serum. On the basis of these features and the suggested function of AI-BP in cholesterol transport in higher eukaryotes, we propose a role for EmABP in cholesterol and lipid uptake mechanisms of larval E. multilocularis.

show abstract

Section: Vol 77 2009 Echinococcus Apolipoprotein A-i Binding Proteimentioning

confidence: 96%

Molecular Characterization of EmABP, an Apolipoprotein A-I Binding Protein Secreted by the Echinococcus multilocularis Metacestode

Bernthaler

Epping

Schmitz³

et al. 2009

Infect Immun

View full text Add to dashboard Cite

show abstract

“…Although various immunomodulatory proteins have been isolated and characterized, the signature E. granulosus antigens in hydatid cyst fluid are still antigen 5 and antigen B (AgB) (39,40,58). Antigen 5, a 67-kDa glycoprotein, and especially AgB, a 160-kDa lipoprotein, are the major immunodominant antigens and are thought to be responsible for the immunomodulatory activities of E. granulosus, promoting its survival within a mammalian host (3,10,13,22,28,32). In our previous studies investigating the cellular response in human CE, we found that sheep hydatid fluid (SHF) elicits both T helper 1 (Th1) and Th2 cell activation (49,50).…”

Section: Dcs From Healthy Human Donors During Monocyte Differentiatimentioning

confidence: 99%

Echinococcus granulosus Antigen B Impairs Human Dendritic Cell Differentiation and Polarizes Immature Dendritic Cell Maturation towards a Th2 Cell Response

et al. 2007

View full text Add to dashboard Cite

Despite inducing a strong host cellular and humoral immune response, the helminth Echinococcus granulosus is a highly successful parasite that develops, progresses, and ultimately causes chronic disease. Although surgery remains the preferred therapeutic option, pharmacological research now envisages antihelminthic strategies. To understand the mechanisms that E. granulosus uses to escape host immunosurveillance and promote chronic infection, we investigated how two hydatid cyst components, purified antigen B (AgB) and sheep hydatid fluid (SHF), act on host dendritic cell (DC) differentiation from monocyte precursors and how they influence maturation of DC that have already differentiated. We evaluated the immunomodulatory potential of these antigens by performing immunochemical and cytofluorimetric analyses of monocyte-derived DCs from healthy human donors. During monocyte differentiation, AgB and SHF downmodulated CD1a expression and upregulated CD86 expression. Compared with immature DCs differentiated in medium alone (iDCs), AgB-and SHF-differentiated cells stimulated with lipopolysaccharide included a significantly lower percentage of CD83؉ cells (P < 10 ؊4 ) and had weaker costimulatory molecule expression. When stimulated with AgB and SHF, iDCs matured and primed lymphocytes towards the Th2 response typical of E. granulosus infection. SHF and particularly AgB reduced the production of interleukin-12p70 (IL-12p70) and tumor necrosis factor alpha in lipopolysaccharide-stimulated iDCs. Anti-IL-10 antibodies increased the levels of IL-12p70 secretion in AgB-and SHF-matured DCs. AgB and SHF induced interleukin-1 receptor-associated kinase phosphorylation and activated nuclear factor-B, suggesting that Toll-like receptors could participate in E. granulosus-stimulated DC maturation. These results suggest that E. granulosus escapes host immunosurveillance in two ways: by interfering with monocyte differentiation and by modulating DC maturation.

show abstract

“…The 8 kDa antigen has been shown to be hydatid specific. Antigen B which comprises 8 and 24 kDa may have the opportunity to accumulate in the cyst fluid after being secreted by the parasite in such a way that the protein has the chance to aggregate into a form that is more immunogenic before the antigen gains contact with the host immune system (Mamuti et al 2006). …”

Section: Resultsmentioning

confidence: 99%

“…In order to overcome these difficulties various novel tests using purified antigens are essential for confirmative diagnosis of hydatidosis in man and animals. Currently, the antigen B, hydatid cyst fluid and these properties have encouraged the preferential use of this antigen over other hydatid antigens, in the sero diagnosis of CE (Maddison et al 1989;Fernandez et al 1996;Mamuti et al 2006;Jiang et al 2012). Native antigens and their purified subunit fractions are more reliable for serodiagnostic purposes than recombinant proteins and synthetic peptides .…”

Section: Introductionmentioning

confidence: 99%

Diagnosis of cystic echinococcosis in buffaloes by native 8 kDa antigen using latex agglutination test (LAT)

2015

View full text Add to dashboard Cite

The dog tapeworm Echinococcus granulosus is the causative agent of cystic hydatid disease in domestic/ wild herbivores animals and man. Accurate immunodiagnosis of the infection requires highly specific and sensitive antigens. The aim of this study was to develop and evaluate immunoassays with principles of precipitation, agglutination for the identification of buffaloes infected with hydatid cyst which would allow the monitoring of animals from endemic areas and identifying infected animals prior to slaughter. The immunoassays were developed and validated using hydatid specific, non-cross reactive low molecular weight 8 kDa hydatid cyst fluid protein. Sera used for the assay validations were obtained from 200 buffaloes infected naturally with hydatid cyst and 200 noninfected buffaloes. The diagnostic sensitivity with latex agglutination test was 98.67 %. It should be useful for the conformation of hydatid cyst infected individual sheep.

show abstract

Recent advances in characterization of Echinococcus antigen B

Cited by 52 publications

References 32 publications

Molecular Characterization of EmABP, an Apolipoprotein A-I Binding Protein Secreted by the Echinococcus multilocularis Metacestode

Molecular Characterization of EmABP, an Apolipoprotein A-I Binding Protein Secreted by the Echinococcus multilocularis Metacestode

Echinococcus granulosus Antigen B Impairs Human Dendritic Cell Differentiation and Polarizes Immature Dendritic Cell Maturation towards a Th2 Cell Response

Diagnosis of cystic echinococcosis in buffaloes by native 8 kDa antigen using latex agglutination test (LAT)

Contact Info

Product

Resources

About