Molecular cloning of a rhoptry protein (ROP6) secreted from Toxoplasma gondii.
10.3347/kjp.2006.44.3.251
- Author:
Hye Jin AHN
1
;
Sehra KIM
;
Ho Woo NAM
Author Information
1. Department of Parasitology and the Catholic Institute of Parasitic Diseases, College of Medicine, Catholic University of Korea, Seoul 137-701, Korea. howoo@catholic.ac.kr
- Publication Type:Original Article ; Research Support, Non-U.S. Gov't
- Keywords:
Toxoplasma gondii;
excretory/secretory proteins;
ROP6;
cDNA sequence;
hydrophilic domain
- MeSH:
Toxoplasma/enzymology/*genetics;
Protozoan Proteins/*genetics/metabolism;
Peptide Hydrolases/genetics/metabolism;
Molecular Sequence Data;
Gene Library;
Cloning, Molecular;
Animals;
Amino Acid Sequence;
3' Untranslated Regions
- From:The Korean Journal of Parasitology
2006;44(3):251-254
- CountryRepublic of Korea
- Language:English
-
Abstract:
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 3'-UTR was probed in a T. gondii cDNA expression library. A full length cDNA sequence of the rhoptry protein was completed after 5'-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.
