Increasing the expression levels of papillomavirus major capsid protein in Escherichia coli by N-terminal deletion.
The major capsid protein L1 of human papillomavirus (HPV) contains the immunodominant neutralization epitopes of the virus and can auto-assembles to form virus-like particles (VLPs). Therefore, HPV L1 capsid proteins have been well investigated as potential vaccine candidates. To express large quantities of human papillomavirus type 16 (HPV-16) L1 in Escherichia coli (E. coli), The HPV-16 L1 gene was cloned into pGEX-4T-1, resulting in only low expression levels of HPV-16 L1 in E. coli. The first 129 nucleotides of the 5' end of the L1 gene, which contains the major inhibitory RNA element, were then deleted. The deletion RNA was efficiently translated, resulting in about 2-fold higher L1 accumulation in E. coli. The N-terminal amino-acid deletion did not affect the ability of L1 to auto-assemble in E. coli and form small VLPs.
Ma
Zhenghai
Z
College of Life Science and Technology, Xinjiang University, 14# Shengli Road, Urumchi 830046, China.
Chen
Bangdang
B
Zhang
Fuchun
F
Yu
Meng
M
Liu
Tingting
T
Liu
Lihong
L
D036022:Capsid Proteins / Q000096:biosynthesis*; D004926:Escherichia coli / Q000378:metabolism*; D002479:Inclusion Bodies / Q000378:metabolism; D046529:Microscopy, Electron, Transmission; D009856:Oncogene Proteins, Viral / Q000096:biosynthesis*; D010957:Plasmids; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis
D036022:Capsid Proteins; D009856:Oncogene Proteins, Viral; D011993:Recombinant Fusion Proteins; C063317:L1 protein, Human papillomavirus type 16