[Cloning and expression of Cysticercus cellulosae antigen cC1 in E. coli].
OBJECTIVE
To clone and express Cysticercus Cellulosae antigen cC1 in E. coli.


METHODS
cC1 cDNA fragment was cloned to BamHI and PstI sites of pGEM-3Z vector. After alteration of the restriction sites, the fragment was cloned to EcoRI and XhoI sites of pGEX-5T with a synthetic linker to construct recombinant expression vector pGEX-5T-cC1.


RESULTS
The clone produced the largest yield of cC1 protein expression when incubated in 2YT culture medium for 3 h or induced by IPTG for 6 h. Detected by scanning optical densitometry, cC1 constituted 57% of the total bacterial proteins. Western blotting analysis revealed that the GST-cC1 fusion protein exhibited a specific reactive band.


CONCLUSIONS
High level expression of Cysticercus cellulosae antigen cC1 was obtained in E. coli.
Chen
R W
RW
Department of Medical Genetics, Second Military Medical University, Shanghai 200433.
Lin
Y
Y
Sun
S H
SH
D000818:Animals; D000947:Antigens, Helminth / Q000096:biosynthesis* / Q000235:genetics; D003001:Cloning, Molecular; D003552:Cysticercus / Q000276:immunology*; D004926:Escherichia coli / Q000235:genetics*; D005822:Genetic Vectors; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis* / Q000235:genetics; D013552:Swine
D000947:Antigens, Helminth; D011993:Recombinant Fusion Proteins