[Efficient expression of human papillomavirus type 16 (HPV16) capsid proteins L1 and L2 in E. coli].
OBJECTIVE
To study the expression of HPV16 capsid proteins L1 and L2 in E. coli.


METHODS
The plasmids pET-30a-L1 and pET-30a-L2 were constructed from the pET-30a vector, and transducted into the BL21. The fusion proteins 6 x His-L1 and 6 x His-L2 were expressed when induced by adding of IPTG. SDS-PAGE and Western blot analyses were used to detect the expressed proteins.


RESULTS
Fusion proteins 6 x His-L1 and 6 x His-L2 were expressed efficiently in E. coli, the Mr were about 60,000 and 97,000 respectively, 6 x His-L1 degraded more than 6 x His-L2.


CONCLUSIONS
L1 and L2 proteins were expressed at a high level in prokaryotic expression system, and 12 protein were more stable than L1 protein.
Wang
W
W
Beijing Friendship Hospital, Beijing 100050.
Zhou
L
L
Sun
Y
Y
D036022:Capsid Proteins / Q000096:biosynthesis* / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D009856:Oncogene Proteins, Viral / Q000096:biosynthesis* / Q000235:genetics; D027383:Papillomaviridae / Q000235:genetics*; D010957:Plasmids; D014162:Transfection
D036022:Capsid Proteins; C063316:L2 protein, Human papillomavirus type 16; D009856:Oncogene Proteins, Viral; C063317:L1 protein, Human papillomavirus type 16