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

Author:

Riggs Michael W.1,McNeil Michael R.2,Perryman Lance E.3,Stone Alice L.1,Scherman Michael S.2,O’Connor Roberta M.4

Affiliation:

1. Department of Veterinary Science and Microbiology, University of Arizona, Tucson, Arizona 857211;

2. Department of Microbiology, Colorado State University, Fort Collins, Colorado 805232;

3. Department of Microbiology, Pathology, and Parasitology, North Carolina State University, Raleigh, North Carolina 276063; and

4. Department of Pathobiology, University of Florida, Gainesville, Florida 326114

Abstract

ABSTRACT 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 α- or β-glycosidases, was determined. Monoclonal antibody 18.44 did not bind antigen treated with β- d -mannosidase but did bind antigen treated with α- d -mannosidase, other α- or β-glycosidases, or a panel of proteases. These data indicated that the target epitope was dependent on terminal β- 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.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Immunology,Microbiology,Parasitology

Reference36 articles.

1. Alving C. R. Immune reactions of lipids and lipid model membranes Antigens. Sela M. 4 1981 Academic Press London United Kingdom

2. Effects of immune colostrum and orally administered antisporozoite monoclonal antibodies on the outcome of Cryptosporidium parvum infections in neonatal mice

3. Isolation of Cryptosporidium oocysts and sporozoites using discontinuous sucrose and isopycnic Percoll gradients;Arrowood M. J.;J. Parasitol.,1987

4. Immunofluorescent microscopical visualization of trails left by gliding Cryptosporidium parvum sporozoites;Arrowood M. J.;J. Parasitol.,1991

5. Cryptosporidium parvum merozoites share neutralization-sensitive epitopes with sporozoites;Bjorneby J. M.;J. Immunol.,1990

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