Identification of in vivo released products of Onchocerca with diagnostic potential, and characterization of a dominant member, the OV1CF intermediate filament

Cho-Ngwa, Fidelis; Zhu, Xiang; Metuge, Jonathan Alunge; Daggfeldt, Annika; Grönvik, Kjell-Olov; Orlando, Ron; Atwood, James; Titanji, Vincent P. K.

doi:10.1016/j.meegid.2010.08.004

Cited by 7 publications

(4 citation statements)

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“…Thus, like Cho-Ngwa et al (2011), in the present study we also found prominent protein bands between 40 and 70 and 90 kDa, in particular for ES from male filariae (Fig. 1b ) which may comprise the dominant protein OV1CF of 62.4 kDa reported by Cho-Ngwa et al [ 35 ]. This indicates that these proteins may be released from living males or females in the nodule.…”

Section: Discussionsupporting

confidence: 90%

“…For O. volvulus , partially similar protein bands had been observed by Sakwe et al [ 33 ] as at 10–20 kDa, about 40 kDa and 60 kDa . Cho-Ngwa et al [ 35 ] analyzing nodular fluid proteins, so-called in vivo ES products of O. ochengi , observed partially similar protein bands. Thus, like Cho-Ngwa et al (2011), in the present study we also found prominent protein bands between 40 and 70 and 90 kDa, in particular for ES from male filariae (Fig.…”

Section: Discussionmentioning

confidence: 99%

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Onchocerca - infected cattle produce strong antibody responses to excretory-secretory proteins released from adult male Onchocerca ochengi worms

et al. 2018

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BackgroundThe front line molecules from filarial worms and other nematodes or helminthes are their Excretory-Secretory (ES) products. Their interaction with the host cells, proteins and immune system accounts for the skin and eye pathology or hyposensitivity observed in human onchocerciasis. ES products and adult worms’ crude extracts from Onchocerca ochengi, a filarial nematode that infects the African zebu cattle, were utilized in the present study as a model for studying Onchocerca volvulus that causes river blindness in man.MethodsThe ES products were generated from adult male and female worms in vitro and analyzed with poly acrylamide gel electrophoresis (PAGE) and enzyme-linked immunosorbent assay (ELISA) using sera from Onchocerca-infected cattle and humans. The cattle sera were collected from a herd that had been exposed for six years to natural transmission of Onchocerca spp. The expressed reactivity was evaluated and differences analyzed statistically using Kruskal-Wallis rank and Chi-square tests.ResultsThe gel electrophoretic analyses of 156 ES products from O. ochengi female and male worms and of two somatic extracts from three females and 25 males revealed differences in the protein pattern showing pronounced bands at 15, 30–50 and 75 kDa for male ES proteins and 15, 25 and 40–75 kDa for somatic extracts, respectively and less than 100 kDa for female worms. Proteins in the ES products and somatic extracts from female and male Onchocerca ochengi worms were recognized by IgG in sera from both Onchocerca-exposed cattle and humans. Bovine serum antibodies reacted more strongly with proteins in the somatic extracts than with those in the ES products. Interestingly, the reaction was higher with male ES products than with ES products from female worms, suggesting that the males which migrate from one nodule to another are more exposed to the host immune system than the females which remain encapsulated in intradermal nodules.ConclusionsThis study demonstrates that O. ochengi ES products and, in particular, extracts from male filariae may represent a good source of immunogenic proteins and potential vaccine candidates.

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Section: Discussionsupporting

confidence: 90%

Section: Discussionmentioning

confidence: 99%

Onchocerca - infected cattle produce strong antibody responses to excretory-secretory proteins released from adult male Onchocerca ochengi worms

et al. 2018

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“…Evidence is not available on the anatomical localization of exosomes in parasitic nematode secretory systems, but many proteins detected in nematode secretomes, including actin, elongation factors, aldolase, enolase, HSP70 and cyclophilin, are common components of mammalian exosomes (http://www.exocarta.org/exosome_markers). A recent report identified 27 Onchocerca ochengi proteins recovered from nodules [36], including many homologs of secretome proteins in other filariae. The majority of the O. ochengi proteins lacked secretion signals and are associated with exosomes in other organisms; these data support the relevance of the antigens detected in vitro and suggest that the role of exosomes, as a source of secreted proteins, warrants further investigation.…”

Section: Discussionmentioning

confidence: 99%

First analysis of the secretome of the canine heartworm, Dirofilaria immitis

et al. 2012

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BackgroundThe characterization of proteins released from filariae is an important step in addressing many of the needs in the diagnosis and treatment of these clinically important parasites, as well as contributing to a clearer understanding of their biology. This report describes findings on the proteins released during in vitro cultivation of adult Dirofilaria immitis , the causative agent of canine and feline heartworm disease. Differences in protein secretion among nematodes in vivo may relate to the ecological niche of each parasite and the pathological changes that they induce.MethodsThe proteins in the secretions of cultured adult worms were run on Tris-Glycine gels, bands separated and peptides from each band analysed by ultra mass spectrometry and compared with a FastA dataset of predicted tryptic peptides derived from a genome sequence of D. immitis. ResultsThis study identified 110 proteins. Of these proteins, 52 were unique to D. immitis . A total of 23 (44%) were recognized as proteins likely to be secreted. Although these proteins were unique, the motifs were conserved compared with proteins secreted by other nematodes.ConclusionThe present data indicate that D. immitis secretes proteins that are unique to this species, when compared with Brugia malayi. The two major functional groups of molecules represented were those representing cellular and of metabolic processes. Unique proteins might be important for maintaining an infection in the host environment, intimately involved in the pathogenesis of disease and may also provide new tools for the diagnosis of heartworm infection.

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“…Furthermore, the immunomodulatory properties of helminth ESPs and their potential use to treat allergy and autoimmune diseases [26,27] as well as metabolic syndrome have been reported [28]. The exploitation of ESPs of Onchocerca in the search for novel drugs, vaccines, diagnostics as well as mediators of immune response have also been described [29–33]. Given that the Onchocerca nodule is known to be vascularized [34,35], such molecules could reach host circulation thereby supporting investigations towards the detection of O .…”

Section: Introductionmentioning

confidence: 99%

Identification and characterization of the Onchocerca volvulus Excretory Secretory Product Ov28CRP, a putative GM2 activator protein

et al. 2019

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Onchocerca volvulus is the nematode pathogen responsible for human onchocerciasis also known as “River blindness”, a neglected tropical disease that affects up to 18 million people worldwide. Helminths Excretory Secretory Products (ESPs) constitute a rich repertoire of molecules that can be exploited for host-parasite relationship, diagnosis and vaccine studies. Here, we report, using a range of molecular techniques including PCR, western blot, recombinant DNA technology, ELISA, high performance thin-layer chromatography and mass spectrometry that the 28 KDa cysteine-rich protein (Ov28CRP) is a reliable component of the O . volvulus ESPs to address the biology of this parasite. We showed that (1) Ov28CRP is a putative ganglioside GM2 Activator Protein (GM2AP) conserved in nematode; (2) OvGM2AP gene is transcriptionally activated in all investigated stages of the parasitic life cycle, including larval and adult stages; (3) The full-length OvGM2AP was detected in in-vitro O . volvulus ESPs of adult and larval stages; (4) the mass expressed and purified recombinant OvGM2AP purified from insect cell culture medium was found to be glycosylated at asparagine 173 and lacked N-terminal signal peptide sequence; (5) the recombinant OvGM2AP discriminated serum samples of infected and uninfected individuals; (6) OvGM2AP competitively inhibits MUG degradation by recombinant β-hexosaminidase A but not MUGS, and could not hydrolyze the GM2 to GM3; (7) humoral immune responses to the recombinant OvGM2AP revealed a negative correlation with ivermectin treatment. Altogether, our findings suggest for the first time that OvGM2AP is an antigenic molecule whose biochemical and immunological features are important to gain more insight into our understanding of host-parasite relationship, as well as its function in parasite development at large.

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Identification of in vivo released products of Onchocerca with diagnostic potential, and characterization of a dominant member, the OV1CF intermediate filament

Cited by 7 publications

References 15 publications

Onchocerca - infected cattle produce strong antibody responses to excretory-secretory proteins released from adult male Onchocerca ochengi worms

Onchocerca - infected cattle produce strong antibody responses to excretory-secretory proteins released from adult male Onchocerca ochengi worms

First analysis of the secretome of the canine heartworm, Dirofilaria immitis

Identification and characterization of the Onchocerca volvulus Excretory Secretory Product Ov28CRP, a putative GM2 activator protein

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