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Infection and Immunity, February 2004, p. 980-987, Vol. 72, No. 2
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.2.980-987.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

The Cryptosporidium Oocyst Wall Protein Is a Member of a Multigene Family and Has a Homolog in Toxoplasma

Thomas J. Templeton,1 Cheryl A. Lancto,2 Vladimir Vigdorovich,2 Chang Liu,2 Nicole R. London,2 Kelly Z. Hadsall,2 and Mitchell S. Abrahamsen2*

Department of Microbiology and Immunology, Weill Medical College of Cornell University, New York, New York 10021,1 Department of Veterinary PathoBiology, University of Minnesota, St. Paul, Minnesota 551082

Received 29 April 2003/ Returned for modification 22 July 2003/ Accepted 20 October 2003

Coccidian parasites are transmitted via a fecal oocyst stage that is exceptionally resistant to environmental stress and harsh chemical treatments, which allows parasites to stably persist outside a host. Because of its oocyst durability Cryptosporidium parvum is a significant water- and food-borne pathogen of humans, as well as animals of agricultural importance. To date, only one apicomplexan oocyst membrane protein has been identified, Cryptosporidium oocyst wall protein 1 (COWP1). COWP1 has a highly cysteine-rich periodicity due to arrays of two apicomplexan-specific motifs, designated the type I and type II domains. In this study, exhaustive BLAST screening of a complete C. parvum genome sequence database resulted in identification of eight additional genes encoding similar arrays of cysteine-rich type I and/or type II domains. Transcript expression analysis revealed that all COWP genes are abundantly expressed at a time when developing oocysts are observed, roughly 48 to 72 h after inoculation of in vitro cultures. A monoclonal antibody recognizing COWP8 specifically localized to the C. parvum oocyst wall, supporting the hypothesis that multiple COWPs play a role in the oocyst wall structure. BLAST screening of the Toxoplasma gondii genome sequence database resulted in identification of a gene encoding at least one COWP homolog (TgOWP1), and this multiexon sequence information was used to isolate a full-length cDNA. Exhaustive screening of Plasmodium sp. genome sequence databases by using COWP genes as BLAST queries failed to detect similar proteins in Plasmodium. We therefore propose that the COWP family of proteins have a structural role in apicomplexan species that produce durable shed cysts capable of surviving environmental stress.


* Corresponding author. Mailing address: Department of Veterinary PathoBiology, University of Minnesota, St. Paul, MN 55108. Phone: (612) 624-1244. Fax: (612) 625-0204. E-mail: abe{at}umn.edu.

Editor: S. H. E. Kaufmann


Infection and Immunity, February 2004, p. 980-987, Vol. 72, No. 2
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.2.980-987.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.




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