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Increasing the expression levels of papillomavirus major capsid protein in Escherichia coli by N-terminal deletion.

Abstract：

: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.

journal_name

Protein Expr Purif

journal_title

Protein expression and purification

authors

Ma Z,Chen B,Zhang F,Yu M,Liu T,Liu L

doi

10.1016/j.pep.2007.05.010

subject

Has Abstract

pub_date

2007-11-01 00:00:00

pages

72-9

issue

1

eissn

1046-5928

issn

1096-0279

pii

S1046-5928(07)00150-7

journal_volume

56

pub_type

杂志文章

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