Shorten human papilloma virus 16 type L1 protein

Abstract

The invention relates to a truncated human papillomavirus type 16 L1 protein, virus-like particles composed of the protein, a vaccine containing the virus-like particles, and an application thereof in preventing cervical cancer.

Description

technical field The invention relates to a truncated human papillomavirus type 16 L1 protein, a virus-like particle composed of it, a vaccine containing the virus-like particle and its use in preventing cervical cancer. Background technique Human papillomavirus HPV (Human Papillomavirus) is a non-enveloped DNA virus belonging to the family Papovaviridae. The viral genome is a double-stranded closed circular DNA with a size of about 7.2-8 kb and 8 open frames. The genome can be divided into three regions according to different functions: ① early region (E), about 4.5kb, encoding E1, E2, E4-E76 non-structural proteins related to virus replication, transcription and transformation; ② late region (L ), about 2.5kb, encoding major capsid protein L1 and minor capsid protein L2; ③Long regulatory region (LCR), located between the end of the L region and the beginning of the E region, about 800-900bp long, does not encode any protein , containing DNA replication, expression control...

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Problems solved by technology

However, because most of the HPV L1 protein expressed by E. coli loses its natural conformation, it cannot produce protective antibodies against HPV.

Or the above-mentioned protein can also obtain HPV VLP (Kelsall, S.R. and J.K.Kulski (1995). JVirol Methods 53 (1): 75-90) through inclusion body purification, renaturation and other steps, but the amount of protein loss in the renaturation process Large, low yield, difficult to apply in large-scale production

Although HPV L1 protein can also be solublely expressed in the correct conformation in E. coli and dissolved in the lysed supernatant of the bacteria, the expression level is low, and there are many types and large amounts of foreign proteins in the supernatant, so it is necessary to purify the target protein from it. Protein is quite difficult

Although there are also reports in the literature that the expression of L1 protein in the supernatant can be increased by means of GST fusion expression, and it can help the purification of the target protein (Li, M., T.P.Cripe, etal. (1997). J Virol 71 (4): 2988-95.), but the cleavage of fusion proteins often requires expensive enzymes, which still cannot be applied to large-scale production

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