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Infection and Immunity, July 2000, p. 4108-4116, Vol. 68, No. 7
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Molecular Cloning and Expression of a Gene Encoding Cryptosporidium parvum Glycoproteins gp40 and gp15

Ana Maria Cevallos,1 Xiaoping Zhang,1 Matthew K. Waldor,1 Smitha Jaison,1 Xiaoyin Zhou,2 Saul Tzipori,1,3 Marian R. Neutra,2 and Honorine D. Ward1,3,*

Division of Geographic Medicine and Infectious Diseases, New England Medical Center, Tufts University School of Medicine, Boston, Massachusetts 021111; Division of Infectious Diseases, Tufts University School of Veterinary Medicine, North Grafton, Massachusetts 015363; and GI Cell Biology Laboratory, Children's Hospital and Harvard Medical School, Boston, Massachusetts 021152

Received 7 January 2000/Accepted 1 April 2000

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. 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.

* Corresponding author. Mailing address: New England Medical Center, Division of Geographic Medicine and Infectious Diseases, 750 Washington St., NEMC Box 041, Boston, MA 02111. Phone: (617) 636-7032. Fax: (617) 636-5292. E-mail: hward{at}lifespan.org.

Infection and Immunity, July 2000, p. 4108-4116, Vol. 68, No. 7
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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