Antigen incorporation on Cryptosporidium parvum oocyst walls

Entrala, Emilio; Sbihi, Younes; SÆnchez-Moreno, Manuel

doi:10.1590/s0074-02762001000200016

Cited by 5 publications

(6 citation statements)

References 7 publications

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“…Therefore, materials that were previously located within the macrogamont were later transferred into the outer oocyst wall. This result is in agreement with the findings of Bonnin et al (1991) and Entrala et al (2001), but with the difference that, in the present study, the WF I antigens were directly incorporated into the outer oocyst wall while, in the case of Cryptosporidium, the electronlucent vesicles were released into the parasitophorous vacuole and later incorporated in the outer oocyst wall (Bonnin et al 1991).…”

Section: Characterization Of the Antigens Recognized By Mab E1d8supporting

confidence: 93%

Monoclonal antibodies specific for the two types of wall-forming bodies of Eimeria tenella macrogametes (Coccidia, Apicomplexa)

Mouafo

Weck-Heimann

Dubremetz

et al. 2002

Parasitology Research

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Two monoclonal antibodies (mAbs) raised against the macrogamonts of Eimeria tenella identified antigens located in the wall-forming bodies of type I (WF I) and type II (WF II) by indirect immunofluorescence and by immunoelectron microscopy. With these mAbs, the involvement of both types of wall-forming body at the protein level in the formation of the inner and outer oocyst walls of E. tenella was shown by indirect immunofluorescence assay. On Western blots of pure macrogamont, mAb E1D8 against WF I reacted with a series of bands between 42 kDa and 105 kDa. In pure, unsporulated extract, this mAb recognized a complex of bands between 26 kDa and 153 kDa. mAb E2E5 against WF II, on Western blots of pure extract of macrogamonts, recognized an antigen of 51 kDa. Later in the development, after the formation of the inner oocyst wall, mAb E2E5 reacted with three polypeptide of 23, 25 and 30 kDa. Proteolytic processing may be forwarded as the mechanism regulating the distinct regulation protein involved in the oocyst wall.

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Section: Characterization Of the Antigens Recognized By Mab E1d8supporting

confidence: 93%

Monoclonal antibodies specific for the two types of wall-forming bodies of Eimeria tenella macrogametes (Coccidia, Apicomplexa)

Mouafo

Weck-Heimann

Dubremetz

et al. 2002

Parasitology Research

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“…The weakly glycosylated, proteasesensitive, moderately electron-dense inner layer of the wall contains COWPs, as previously shown (33). The fibrillar tethers, which appear to connect the sporozoite to the oocyst wall, collapse into electron-dense globules that have also been called "knobs" (11). Antibodies to two mucins bind to the tethers (anti-gp900 and anti-gp40), while antibodies to O-linked GalNAc bind to globules.…”

Section: Vol 9 2010mentioning

confidence: 76%

“…attached to sporozoites, the fibrils appear to collapse into electron-dense globules, which resemble "knobs" stained by anti-C. parvum antibodies (11). Because these ruthenium red-stained fibrils appear to attach the sporozoites to the inner surface of the oocyst wall, we will refer to them as "tethers.…”

Section: Resultsmentioning

confidence: 99%

“…The fibrillar tethers (red), which appear to connect the sporozoite to the oocyst wall, include two mucins (gp900 and gp40). These fibrils likely collapse into electron-dense globules, which have also been called "knobs" (11) that stain with antibodies to O-linked GalNAc.…”

Section: Vol 9 2010mentioning

confidence: 99%

“…COWPs, which have homologues in Toxoplasma, are a family of nine proteins that contain polymorphic Cys-rich and Hisrich repeats (37,46). Finally, on the inner surface of C. parvum oocyst walls are knob-like structures, which cross-react with an anti-oocyst monoclonal antibody (11).…”

mentioning

confidence: 99%

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Evidence for Mucin-Like Glycoproteins That Tether Sporozoites of Cryptosporidium parvum to the Inner Surface of the Oocyst Wall

et al. 2010

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Cryptosporidium parvum oocysts, which are spread by the fecal-oral route, have a single, multilayered wall that surrounds four sporozoites, the invasive form. The C. parvum oocyst wall is labeled by the Maclura pomifera agglutinin (MPA), which binds GalNAc, and the C. parvum wall contains at least two unique proteins (Cryptosporidium oocyst wall protein 1 [COWP1] and COWP8) identified by monoclonal antibodies. C. parvum sporozoites have on their surface multiple mucin-like glycoproteins with Ser-and Thr-rich repeats (e.g., gp40 and gp900). Here we used ruthenium red staining and electron microscopy to demonstrate fibrils, which appear to attach or tether sporozoites to the inner surface of the C. parvum oocyst wall. When disconnected from the sporozoites, some of these fibrillar tethers appear to collapse into globules on the inner surface of oocyst walls. The most abundant proteins of purified oocyst walls, which are missing the tethers and outer veil, were COWP1, COWP6, and COWP8, while COWP2, COWP3, and COWP4 were present in trace amounts. In contrast, MPA affinity-purified glycoproteins from C. parvum oocysts, which are composed of walls and sporozoites, included previously identified mucin-like glycoproteins, a GalNAc-binding lectin, a Ser protease inhibitor, and several novel glycoproteins (C. parvum MPA affinity-purified glycoprotein 1 [CpMPA1] to CpMPA4). By immunoelectron microscopy (immuno-EM), we localized mucin-like glycoproteins (gp40 and gp900) to the ruthenium red-stained fibrils on the inner surface wall of oocysts, while antibodies to the O-linked GalNAc on glycoproteins were localized to the globules. These results suggest that mucin-like glycoproteins, which are associated with the sporozoite surface, may contribute to fibrils and/or globules that tether sporozoites to the inner surface of oocyst walls.

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It's official – Cryptosporidium is a gregarine: What are the implications for the water industry?

et al. 2016

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Parasites of the genus Cryptosporidium are a major cause of diarrhoea and ill-health in humans and animals and are frequent causes of waterborne outbreaks. Until recently, it was thought that Cryptosporidium was an obligate intracellular parasite that only replicated within a suitable host, and that faecally shed oocysts could survive in the environment but could not multiply. In light of extensive biological and molecular data, including the ability of Cryptosporidium to complete its life cycle in the absence of a host and the production of novel extracellular stages, Cryptosporidium has been formally transferred from the Coccidia, to a new subclass, Cryptogregaria, with gregarine parasites. In this review, we discuss the close relationship between Cryptosporidium and gregarines and discuss the implications for the water industry.

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Antigen incorporation on Cryptosporidium parvum oocyst walls

Cited by 5 publications

References 7 publications

Monoclonal antibodies specific for the two types of wall-forming bodies of Eimeria tenella macrogametes (Coccidia, Apicomplexa)

Monoclonal antibodies specific for the two types of wall-forming bodies of Eimeria tenella macrogametes (Coccidia, Apicomplexa)

Evidence for Mucin-Like Glycoproteins That Tether Sporozoites of Cryptosporidium parvum to the Inner Surface of the Oocyst Wall

It's official – Cryptosporidium is a gregarine: What are the implications for the water industry?

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