Molecular cloning of a rhoptry protein (ROP6) secreted from Toxoplasma gondii.
Monoclonal antibody (mAb) Tg786 against Toxoplasma gondii has been found to detect a 42-kDa rhoptry protein (ROP6) which showed protease activity and host cell binding characteristics after secretion. Using the mAb, a colony containing a 3o-UTR was probed in a T. gondii cDNA expression library. A full length cDNA sequence of the rhoptry protein was completed after 5o-RACE, which consisted of 1,908 bp with a 1,443 bp ORF. The deduced amino acid sequence of ROP6 consisted of a polypeptide of 480 amino acids without significant homology to any other known proteins. This sequence contains an amino terminal stop transfer sequence downstream of a short neutral sequence, hydrophilic middle sequence, and hydrophobic carboxy terminus. It is suggested that the ROP6 is inserted into the rhoptry membrane with both N- and C-termini.
Ahn
Hye-Jin
HJ
Department of Parasitology and the Catholic Institute of Parasitic Diseases, College of Medicine, Catholic University of Korea, Seoul, Korea.
Kim
Sehra
S
Nam
Ho-Woo
HW
D020413:3' Untranslated Regions; D000595:Amino Acid Sequence; D000818:Animals; D003001:Cloning, Molecular; D015723:Gene Library; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000235:genetics / Q000378:metabolism; D015800:Protozoan Proteins / Q000235:genetics* / Q000378:metabolism; D014122:Toxoplasma / Q000201:enzymology / Q000235:genetics*
D020413:3' Untranslated Regions; D015800:Protozoan Proteins; D010447:Peptide Hydrolases