Complete Genome Sequence of the Apicomplexan, Cryptosporidium parvum

  title={Complete Genome Sequence of the Apicomplexan, Cryptosporidium parvum},
  author={Mitchell S. Abrahamsen and Thomas J. Templeton and Shinichiro Enomoto and Juan E. Abrahante and Guan Zhu and Cheryl A. Lancto and Mingqi Deng and Chang Liu and Giovanni Widmer and Saul Tzipori and Gregory A. Buck and Ping Xu and A. T. Bankier and Paul H. Dear and Bernard A. Konfortov and H. Spriggs and Lakshminarayan M. Iyer and Vivek Anantharaman and L. Aravind and Vivek Kapur},
  pages={441 - 445}
The apicomplexan Cryptosporidium parvum is an intestinal parasite that affects healthy humans and animals, and causes an unrelenting infection in immunocompromised individuals such as AIDS patients. We report the complete genome sequence of C. parvum, type II isolate. Genome analysis identifies extremely streamlined metabolic pathways and a reliance on the host for nutrients. In contrast to Plasmodium and Toxoplasma, the parasite lacks an apicoplast and its genome, and possesses a degenerate… 

Genome Sequence of Theileria parva, a Bovine Pathogen That Transforms Lymphocytes

The genome sequence of Theileria parva is reported, an apicomplexan pathogen causing economic losses to smallholder farmers in Africa, and its plastid-like genome represents the first example where all apicoplast genes are encoded on one DNA strand.

The genome of Cryptosporidium hominis

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Cryptosporidium parvum infection in cell culture was significantly inhibited by subtilisin inhibitor III and other serine protease inhibitors, emphasizing the importance of the parasite's subtilase for intracellular development and the enzyme's potential as a drug target.

Genomics of apicomplexan parasites

Genetic datasets currently available for apicomplexans are outlined and biological insights that have emerged as a consequence of their analysis are discussed, focusing on areas of metabolism and host invasion that are opening up opportunities for discovering new therapeutic targets.

Cryptosporidium: genomic and biochemical features.

Preliminary Characterization of MEDLE-2, a Protein Potentially Involved in the Invasion of Cryptosporidium parvum

Results support the potential involvement of MEDLE-2 in the invasion of host cells and show the expression of the protein in sporozoites and development stages of Cryptosporidium parvum.

Treatment of Cryptosporidiosis

Understanding the basic mechanisms by which drugs are transported to the parasite and identifying unique targets are important steps in developing effective therapeutic agents.



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

It is proposed that the COWP family of proteins have a structural role in apicomplexan species that produce durable shed cysts capable of surviving environmental stress.

Cryptosporidium parvum appears to lack a plastid genome.

Primers based upon the highly conserved plastid small- or large-subunit rRNA and the tufA-tRNAPhe genes of other members of the phylum Apicomplexa failed to amplify products from intracellular stages of C. parvum, suggesting an alternative evolutionary fate for this organelle in one member of the ApicOMplexa.

Genetic complementation in apicomplexan parasites

It is shown that complementing sequences can be shuttled between parasite genome and bacterial plasmid, providing an efficient tool for the recovery and functional assessment of candidate genes.

Mediation of Cryptosporidium parvumInfection In Vitro by Mucin-Like Glycoproteins Defined by a Neutralizing Monoclonal Antibody

The surface and apical localization of these glycoproteins and the neutralizing effect of the MAb and α-N-acetylgalactosamine-specific lectins strongly implicate these proteins and their glycotopes as playing a role in C. parvum-host cell interactions.

Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi

The DNA sequences of the 11 chromosomes of the ∼2.9-megabase (Mb) genome of Encephalitozoon cuniculi are reported and it is hypothesize that microsporidia have retained a mitochondrion-derived organelle.

Dissecting Apicoplast Targeting in the Malaria Parasite Plasmodium falciparum

Altering the specific charge characteristics in a model transit peptides by site-directed mutagenesis severely disrupted organellar targeting in vivo and putative Hsp70 (DnaK) binding sites present in the transit peptide proved to be important for correct targeting.