Abstract
A 567bp DNA fragment was amplified from Schistosoma japonicum adult worm mRNA by RT-PCR. Sequence analysis revealed that this fragment contained S. Japonicum Chinese strain membrane-associated protein (Sj-22.6) gene. Then this gene was cloned into the expression vector pGEX-4T, and subsequently expressed in Escherichia coli. The recombinant GST-fusion protein was purified by glutathione agarose affinity chromatography. Its molecular weight was about 48 kD. The yield of expression was around 40 mg/L E.coli culture. The immunological test suggested that the recombinant protein had good antigenity which could make a good basis for the research of its immunological function in Schistosomiasis.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Animals
-
Antigens, Helminth / genetics*
-
Antigens, Helminth / isolation & purification
-
Antigens, Helminth / metabolism
-
Base Sequence
-
Blotting, Western
-
Cloning, Molecular
-
Electrophoresis, Polyacrylamide Gel
-
Escherichia coli / genetics
-
Escherichia coli / metabolism*
-
Membrane Proteins / genetics*
-
Membrane Proteins / isolation & purification
-
Membrane Proteins / metabolism
-
Mice
-
Molecular Sequence Data
-
Recombinant Proteins / genetics
-
Recombinant Proteins / isolation & purification
-
Recombinant Proteins / metabolism
-
Reverse Transcriptase Polymerase Chain Reaction
-
Schistosoma japonicum / genetics*
Substances
-
22.6-kDa antigen, Schistosoma japonicum
-
Antigens, Helminth
-
Membrane Proteins
-
Recombinant Proteins