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J. Biol. Chem., Vol. 278, Issue 52, 52212-52222, December 26, 2003

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Characterization of a Low Molecular Weight Glycolipid Antigen from Cryptosporidium parvum^*

Jeffrey W. Priest, Angela Mehlert¶||, Michael J. Arrowood, Michael W. Riggs**, and Michael A. J. Ferguson¶||

From the Division of Parasitic Diseases, Centers for Disease Control and Prevention, Atlanta, Georgia 30341, ^¶Division of Biological Chemistry and Molecular Microbiology, Wellcome Trust Building, University of Dundee, Dundee DD1 4HN, Scotland, United Kingdom, ^**Department of Veterinary Science and Microbiology, University of Arizona, Tucson, Arizona 85721, and the Atlanta Research and Education Foundation, Decatur, Georgia 30033

Cryptosporidium parvum, an Apicomplexan parasite of the mammalian gut epithelium, causes a diarrheal illness in a wide range of hosts and is transmitted by contamination of food or water with oocyst-laden feces from an infected animal. We have identified a glycosylinositol phospholipid from the sporozoite stage of the parasite that is frequently recognized by serum antibodies from human cryptosporidiosis patients. The humoral immune response is dominated by IgG₁ subclass antibodies but can also include IgA and IgM antibodies. The glycosylinositol phospholipids were purified by butanol extraction of a Triton X-114-soluble fraction followed by octyl-Sepharose column chromatography and preparative high performance TLC and were shown to include at least 5 species. By using mass spectrometry and radiolabeled neutral glycan analysis, we found that the structure of the dominant glycosylinositol phospholipid antigen contained a C18:0 lyso-acylglycerol, a C16:0-acylated inositol, and an unsubstituted mannose₃-glucosamine glycan core. Other diacyl species were also identified, most notably a series of glycosylinositol phospholipids having an acyl-linked C20:0 to C28:0 lipid on the inositol ring. Less abundant species having three acyl-linked fatty acids and species with an additional 1–3 hexoses linked to the mannose core were also observed. We are currently working to determine the role that these glycolipids may play in the development of disease and in the clearance of infection.

Received for publication, June 26, 2003 , and in revised form, September 10, 2003.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^|| Supported by Program Grant 071463 from The Wellcome Trust and by HFSP Grant RG00288/2000-M303.

To whom correspondence should be addressed: Division of Parasitic Diseases, Centers for Disease Control and Prevention, 4770 Buford Hwy., NE, Atlanta, GA 30341. Tel.: 770-488-4587; Fax: 770-488-4108; E-mail: jpriest{at}cdc.gov.

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				B. Zeng, X. Cai, and G. Zhu Functional characterization of a fatty acyl-CoA-binding protein (ACBP) from the apicomplexan Cryptosporidium parvum. Microbiology, August 1, 2006; 152(Pt 8): 2355 - 2363. [Abstract] [Full Text] [PDF]