Characterization of a heavy metal ATPase from the apicomplexan Cryptosporidium parvum

Gene
Michael J LaGierJ S Keithly

Abstract

P1-ATPases are transporters which pump heavy metals across membranes, either to provide enzymes with essential cofactors or to remove excess, toxic metal cations from the cytosol. The first protist P1-ATPase (CpATPase2) has been isolated from the apicomplexan Cryptosporidium parvum, an opportunistic pathogen of AIDS patients. This single copy gene encodes 1260 amino acids (aa), predicting a protein of 144.7 kDa. Reverse transcription-polymerase chain reaction (RT-PCR) and western blot analysis confirmed CpATPase2 expression. Immunofluorescence microscopy of C. parvum sporozoites using rabbit antiserum raised against a glutathione-S-transferase (GST) fusion protein suggests that CpATPase2 is associated with the plasma- and cytoplasmic membranes. The protein shares greatest overall sequence similarity to previously characterized copper P1-ATPases. Expression and subsequent biochemical analyses of the N-terminal heavy metal binding domain (HMBD, GMxCxxC) of CpATPase2 as a maltose-binding protein (MBP) in Escherichia coli reveals that the protein specifically binds reduced copper, Cu(I), in vitro and in vivo, and that the cysteine residues of HMBD are responsible for heavy metal coordination. Overall, these data show that the apico...Continue Reading

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Citations

Jun 14, 2002·International Journal for Parasitology·Michael J LaGierG Zhu
Jan 9, 2013·Clinical Microbiology Reviews·Maha BouzidKevin M Tyler
Feb 4, 2009·Experimental Parasitology·Stanley Dean Rider, G Zhu
Jun 28, 2003·FEMS Microbiology Reviews·Dietrich H Nies

Related Concepts

AF134591
DNA-dependent ATPase
Metazoa
Cations
Copper
Cysteine Hydrochloride
Yb-Glutathione-S-Transferase
Plasma Protein Binding Capacity
Hybrid Proteins, Recombinant
Transcription, Genetic

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