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[Efficient expression of human papillomavirus type 16 (HPV16) capsid proteins L1 and L2 in E. coli]
Abstract
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.
Conclusion:
L1 and L2 proteins were expressed at a high level in prokaryotic expression system, and 12 protein were more stable than L1 protein.