Cryptosporidium parvum is a significant cause of diarrheal disease worldwide. The specific molecules that mediate C. Parvum-host cell interactions and the molecular mechanisms involved in the pathogenesis of cryptosporidiosis are unknown.

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In this study we have shown that gp40, a mucin-like glycoprotein, is localized to the surface and apical region of invasive stages of the parasite and is shed from its surface. Gp40-specific antibodies neutralize infection in vitro, and native gp40 binds specifically to host cells, implicating this glycoprotein in C. Parvum attachment to and invasion of host cells. We have cloned and sequenced a gene designated Cpgp40/15 that encodes gp40 as well as gp15, an antigenically distinct, surface glycoprotein also implicated in C. Parvum-host cell interactions. Analysis of the deduced amino acid sequence of the 981-bp Cpgp40/15 revealed the presence of an N-terminal signal peptide, a polyserine domain, multiple predicted O-glycosylation sites, a single potential N-glycosylation site, and a hydrophobic region at the C terminus, a finding consistent with what is required for the addition of a GPI anchor. There is a single copy of Cpgp40/15 in the C.

Parvum genome, and this gene does not contain introns. Our data indicate that the two Cpgp40/15-encoded proteins, gp40 and gp15, are products of proteolytic cleavage of a 49-kDa precursor protein which is expressed in intracellular stages of the parasite. The surface localization of gp40 and gp15 and their involvement in the host-parasite interaction suggest that either or both of these glycoproteins may serve as effective targets for specific preventive or therapeutic measures for cryptosporidiosis. Cryptosporidium parvum, an intestinal apicomplexan parasite, is a significant cause of diarrheal disease worldwide (, ). Download Windows 7 Pro Oa Latam Lenovo there.

Cryptosporidial infection is asymptomatic or self-limiting in immunocompetent hosts, but it may be chronic and life-threatening in immunocompromised patients such as those with AIDS. In children in developing countries, C. Parvum infection has been reported to be associated with persistent diarrheal disease, which may result in subsequent growth impairment (). Recently, this parasite has been implicated as the causative agent of numerous outbreaks of waterborne diarrheal disease (). There is currently no specific therapy approved for the treatment of cryptosporidiosis. Infection with C.

Parvum is initiated by ingestion of oocysts, which undergo excystation to release sporozoites. Sporozoites attach to and invade intestinal epithelial cells, where the parasite undergoes further intracellular development through asexual as well as sexual cycles. Merozoites released into the lumen during the asexual cycle can attach to and invade adjacent epithelial cells and thus maintain intracellular replication. The molecular mechanisms involved in the pathogenesis of cryptosporidiosis and the specific molecules that mediate C.

Parvum-host cell interactions are unknown. A number of C.

Parvum proteins have been implicated in attachment and invasion and are the subject of ongoing investigation (,,,,,,,, ). We have previously identified a monoclonal antibody (MAb), 4E9, that neutralizes C. Parvum infection and inhibits attachment in vitro (A.

Keusch, and H. Ward, submitted for publication). 4E9 was found to recognize two glycoproteins, gp40 and GP900.

Immunofluorescence (IF) studies using this MAb revealed that these glycoproteins are localized to the surface and apical region of sporozoites and merozoites, are shed in trails from sporozoites during gliding motility, and bind to intestinal epithelial cells. The epitope recognized by 4E9 contains α- N-acetylgalactosamine (αGalNAc) residues, which are present in a mucin-type O-glycosidic linkage. Lectins specific for these residues also block attachment in vitro. The gene encoding one of these glycoproteins, GP900, a high-molecular-weight mucin-like glycoprotein, has recently been cloned and sequenced (). In the present study, we have characterized gp40 and cloned, sequenced, and expressed the gene encoding it. The open reading frame (ORF) encoding gp40 also encodes a previously described () 15-kDa surface glycoprotein (gp15) (W.