Two distinct oxysterol binding protein-related proteins in the parasitic protist Cryptosporidium parvum (Apicomplexa). Academic Article

abstract

• Two distinct oxysterol binding protein (OSBP)-related proteins (ORPs) have been identified from the parasitic protist Cryptosporidium parvum (CpORP1 and CpORP2). The short-type CpOPR1 contains only a ligand binding (LB) domain, while the long-type CpORP2 contains Pleckstrin homology (PH) and LB domains. Lipid-protein overlay assays using recombinant proteins revealed that CpORP1 and CpORP2 could specifically bind to phosphatidic acid (PA), various phosphatidylinositol phosphates (PIPs), and sulfatide, but not to other types of lipids with simple heads. Cholesterol was not a ligand for these two proteins. CpOPR1 was found mainly on the parasitophorous vacuole membrane (PVM), suggesting that CpORP1 is probably involved in the lipid transport across this unique membrane barrier between parasites and host intestinal lumen. Although Cryptosporidium has two ORPs, other apicomplexans including Plasmodium, Toxoplasma, and Eimeria possess only a single long-type ORP, suggesting that this family of proteins may play different roles among apicomplexans.

authors

• Zhu, Guan

published proceedings

• Biochem Biophys Res Commun

author list (cited authors)

• Zeng, B., & Zhu, G.

citation count

• 24

complete list of authors

• Zeng, Bin||Zhu, Guran

publication date

• January 2006

publisher

• Elsevier  Publisher

published in

• Biochemical and Biophysical Research Communications  Journal

keywords

• Animals
• Cholesterol
• Cryptosporidium Parvum
• Ligands
• Phosphatidylinositol Phosphates
• Phylogeny
• Protein Binding
• Protozoan Proteins
• Receptors, Steroid
• Recombinant Proteins

Digital Object Identifier (DOI)

• 10.1016/j.bbrc.2006.05.165

start page

• 591

end page

• 599

volume

• 346

issue

• 2

URL

• http%3A%2F%2Fdx.doi.org%2F10.1016%2Fj.bbrc.2006.05.165