Molecular cloning of a rhoptry protein (ROP6) secreted from Toxoplasma gondii
The Korean Journal of Parasitology
;
: 251-254, 2006.
Article
in English
| WPRIM
| ID: wpr-59371
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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Peptide Hydrolases
/
Toxoplasma
/
Molecular Sequence Data
/
Gene Library
/
Protozoan Proteins
/
Amino Acid Sequence
/
Cloning, Molecular
/
3' Untranslated Regions
Limits:
Animals
Language:
English
Journal:
The Korean Journal of Parasitology
Year:
2006
Type:
Article
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