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  • Showing results for Expression[Title] AND Purification[Title] AND Antibody[Title] AND Binding[Title] AND Activity[Title] AND Human[Title] AND 16[Title] AND L1[Title] AND Protein[Title] AND Fused[Title] AND Maltose[Title] AND Binding[Title] AND Protein[Title]. Your search for Expression, Purification, and Antibody Binding Activity of Human Papil-lomavirus 16 L1 Protein Fused to Maltose Binding Protein retrieved no results.
Protein Pept Lett. 2007;14(5):417-24.

Expression, purification, and antibody binding activity of human papillomavirus 16 L1 protein fused to maltose binding protein.

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School of Life Sciences and Biotechnology, Korea University, Anam-dong, Seungbuk-gu, Seoul, South Korea.


Genetic human papillomavirus type 16 L1 (HPV16 L1) has been widely studied for cervical cancer vaccine development. For the enzyme-linked immunosorbent assay (ELISA) screening of these vaccines, HPV16 L1 protein, which is required as a coating protein, has previously been expressed from costly and laborious recombinant baculovirus-infected insect cells. For a novel HPV16 L1 expression system characterized by a high yield of soluble form with simple purification steps, we have cloned and expressed two different types of HPV16 L1, both fused to maltose binding protein (MBP) or glutathione-S-transferase (GST) in Escherichia coli. The yield of soluble HPV16 L1 was influenced by the cultivation temperature. The yield of soluble form in the total MBP-fused HPV16 L1 protein (MBP-HPV16 L1) was 35% at 37 degrees C, but increased to 85% at 22 degrees C. Among the fusion partners, MBP provided higher yields of total and soluble HPV16 L1 than did GST. MBP-HPV16 L1 showed a 4.9-fold higher yield of the soluble form over insoluble inclusion bodies under optimized culture conditions. The soluble form of MBP-HPV16 L1 was purified via MBP affinity chromatography in a recovery yield of 9.7%. After fusion with MBP, HPV16 L1 showed binding activity to HPV16 L1-specific monoclonal antibody comparable to HPV16 L1 from the insect cells in ELISA tests. These results demonstrate that the use of MBP as a fusion partner may generate a high yield of soluble HPV16 L1 under optimized temperature conditions, and that MBP-fused HPV16 L1 might be applied further in evaluations of the immune responses of HPV16 L1-based cervical cancer vaccines.

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