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Infection and Immunity, March 1999, p. 1317-1322, Vol. 67, No. 3
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Cryptosporidium parvum Sporozoite Pellicle Antigen Recognized by a Neutralizing Monoclonal Antibody Is a beta -Mannosylated Glycolipid

Michael W. Riggs,1,* Michael R. McNeil,2 Lance E. Perryman,3 Alice L. Stone,1 Michael S. Scherman,2 and Roberta M. O'Connor4

Department of Veterinary Science and Microbiology, University of Arizona, Tucson, Arizona 857211; Department of Microbiology, Colorado State University, Fort Collins, Colorado 805232; Department of Microbiology, Pathology, and Parasitology, North Carolina State University, Raleigh, North Carolina 276063; and Department of Pathobiology, University of Florida, Gainesville, Florida 326114

Received 1 October 1998/Returned for modification 6 December 1998/Accepted 21 December 1998

The protozoan parasite Cryptosporidium parvum is an important cause of diarrhea in humans, calves, and other mammals worldwide. No approved vaccines or parasite-specific drugs are currently available for the control of cryptosporidiosis. To effectively immunize against C. parvum, identification and characterization of protective antigens are required. We previously identified CPS-500, a conserved, neutralization-sensitive antigen of C. parvum sporozoites and merozoites defined by monoclonal antibody 18.44. In the present study, the biochemical characteristics and subcellular location of CPS-500 were determined. CPS-500 was chloroform extractable and eluted with acetone and methanol in silicic acid chromatography, consistent with being a polar glycolipid. Following chloroform extraction and silicic acid chromatography, CPS-500 was isolated by high-pressure liquid chromatography for glycosyl analysis, which indicated the presence of mannose and inositol. To identify which component of CPS-500 comprised the neutralization-sensitive epitope recognized by 18.44, the ability of the monoclonal antibody to bind CPS-500 treated with proteases, or with alpha - or beta -glycosidases, was determined. Monoclonal antibody 18.44 did not bind antigen treated with beta -D-mannosidase but did bind antigen treated with alpha -D-mannosidase, other alpha - or beta -glycosidases, or a panel of proteases. These data indicated that the target epitope was dependent on terminal beta -D-mannopyranosyl residues. By immunoelectron microscopy, 18.44 binding was localized to the pellicle and an intracytoplasmic tubulovesicular network in sporozoites. Monoclonal antibody 18.44 also bound to antigen deposited and released onto substrate over the course travelled by gliding sporozoites and merozoites. Surface localization, adhesion and release during locomotion, and neutralization sensitivity suggest that CPS-500 may be involved in motility and invasion processes of the infective zoite stages.

* Corresponding author. Mailing address: Department of Veterinary Science and Microbiology, Veterinary Science and Microbiology Bldg., University of Arizona, Tucson, AZ 85721. Phone: (520) 621-8445. Fax: (520) 621-6366. E-mail: mriggs{at}u.arizona.edu.

Infection and Immunity, March 1999, p. 1317-1322, Vol. 67, No. 3
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Priest, J. W., Mehlert, A., Arrowood, M. J., Riggs, M. W., Ferguson, M. A. J. (2003). Characterization of a Low Molecular Weight Glycolipid Antigen from Cryptosporidium parvum. J. Biol. Chem. 278: 52212-52222 [Abstract] [Full Text]  
  • Riggs, M. W., Schaefer, D. A., Kapil, S. J., Barley-Maloney, L., Perryman, L. E. (2002). Efficacy of Monoclonal Antibodies against Defined Antigens for Passive Immunotherapy of Chronic Gastrointestinal Cryptosporidiosis. Antimicrob. Agents Chemother. 46: 275-282 [Abstract] [Full Text]  
  • Langer, R. C., Schaefer, D. A., Riggs, M. W. (2001). Characterization of an Intestinal Epithelial Cell Receptor Recognized by the Cryptosporidium parvum Sporozoite Ligand CSL. Infect. Immun. 69: 1661-1670 [Abstract] [Full Text]  
  • Strong, W. B., Gut, J., Nelson, R. G. (2000). Cloning and Sequence Analysis of a Highly Polymorphic Cryptosporidium parvum Gene Encoding a 60-Kilodalton Glycoprotein and Characterization of Its 15- and 45-Kilodalton Zoite Surface Antigen Products. Infect. Immun. 68: 4117-4134 [Abstract] [Full Text]  
  • Schaefer, D. A., Auerbach-Dixon, B. A., Riggs, M. W. (2000). Characterization and Formulation of Multiple Epitope-Specific Neutralizing Monoclonal Antibodies for Passive Immunization against Cryptosporidiosis. Infect. Immun. 68: 2608-2616 [Abstract] [Full Text]  
  • Langer, R. C., Riggs, M. W. (1999). Cryptosporidium parvum Apical Complex Glycoprotein CSL Contains a Sporozoite Ligand for Intestinal Epithelial Cells. Infect. Immun. 67: 5282-5291 [Abstract] [Full Text]  


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