Determining the protein repertoire of <b><i>Cryptosporidium parvum</i></b> sporozoites

Sanderson, Sanya J.; Xia, Dong; Prieto, H; Yates, John R.; Heiges, Mark; Kissinger, Jessica C.; Bromley, Elizabeth H. C.; Lal, Kalpana; Sinden, Robert E.; Tomley, Fiona M.; Wastling, Jonathan M.

doi:10.1002/pmic.200700804

Cited by 76 publications

(92 citation statements)

References 55 publications

(101 reference statements)

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“…Together, COWPs, which are also present in the predicted proteome of Toxoplasma (37), account for ϳ75% of the C. parvum oocyst wall proteins identified by mass spectroscopy. The relative abundance of C. parvum oocyst wall proteins is in agreement with recent mass spectroscopic analysis of total oocyst proteins, which include proteins from oocyst walls and sporozoites (30).…”

Section: Resultssupporting

confidence: 69%

“…First and most important, these C. parvum proteins are also present in all apicomplexa, including Plasmodium and Theileria, which are transmitted by insect vectors and so do not make an oocyst wall. Second, these glycoproteins were abundant in MPA affinity-purified proteins of C. parvum (below) and/or in mass spectroscopic analyses of sporozoite proteins (30,32).…”

Section: Resultsmentioning

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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Section: Resultssupporting

confidence: 69%

Section: Resultsmentioning

confidence: 99%

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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“…Proteomic analysis of G. duodenalis is still far behind that of other parasitic infections; Plasmodium sp., Leishmania sp., and more recently Toxoplasma gondii and Cryptosporidium parvum, where great inroads have been made into producing functional proteomes of the parasites , Drummelsmith, et al, 2003, El Fakhry, et al, 2002, Nirmalan, et al, 2004, Nugent, et al, 2004. The studies by Xia et al (2008) and Sanderson et al (2008) examining T. gondii and C. parvum respectively are of special note. These studies were both performed using a multi-platform proteomics approach, utilising SDS-PAGE, 2D-PAGE and MudPIT and generated a vast amount of data covering approximately 30% of the predicted proteomes for each organism.…”

Section: Work For the Futurementioning

confidence: 99%

Proteomic analysis of Giardia: Studies from the pre- and post-genomic era

Steuart¹

2010

Experimental Parasitology

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The proteome of Giardia duodenalis has been under study for the last 25 years and has lead to the discovery of valuable information on the biology and variation of the parasite.Proteomic techniques, mainly SDS-PAGE and 2D-PAGE, have been used to investigate protein variation, cellular structure and host parasite interactions. This has allowed for the identification of assemblage and host specific proteins, structural proteins, proteins released by trophozoites upon exposure to host cell monolayers and immunoreactive proteins. These data are important in understanding the pathogenesis of G. duodenalis infections, as well as highlighting potential drug and vaccine targets. There is however a large amount of future work needed to fully understand the proteome of this parasite.

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“…Another advance has been the partial characterization of the proteome of Cryptosporidium sporozoites (70,71) and inclusion of the data in CryptoDB (29) and the proteomics database EPIC DB (43). Availability of reagents such as antibodies from the Albert Einstein Proteomics Resource Center through the Biodefense and Emerging Infections Research Resources Repository (http://www .beiresources.org/) has also facilitated investigation of key Cryptosporidium proteins.…”

Section: Cryptosporidiummentioning

confidence: 99%