Abstract
Recombinant major capsid protein, L1 (M(r) = 55,000), of human papillomavirus type 11 was expressed intracellularly at high levels in a galactose-inducible Saccharomyces cerevisiae expression system by an HPV6/11 hybrid gene. The capsid protein self-assembled into virus-like particles (VLPs) and accounted for 15% of the total soluble protein. A purification process was developed that consisted of two main steps: microfiltration and cation-exchange chromatography. The purified VLPs were 98% homogeneous, and the overall purification yield was 10%. The final product was characterized by several analytical methods and was highly immunogenic in mice.
Copyright 1999 Academic Press.
MeSH terms
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Amino Acids / analysis
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Animals
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Antibody Formation
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Blotting, Western
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Capsid / biosynthesis*
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Capsid / chemistry
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Capsid / immunology
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Capsid / isolation & purification
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Capsid Proteins
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Chromatography, Ion Exchange
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Enzyme-Linked Immunosorbent Assay
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Humans
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Mice
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Mice, Inbred BALB C
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Microscopy, Electron
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Oncogene Proteins, Viral / biosynthesis*
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Oncogene Proteins, Viral / chemistry
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Oncogene Proteins, Viral / immunology
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Oncogene Proteins, Viral / isolation & purification
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Papillomaviridae / chemistry*
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry
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Recombinant Proteins / immunology
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Recombinant Proteins / isolation & purification
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Saccharomyces cerevisiae / metabolism*
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Virus Assembly
Substances
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Amino Acids
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Capsid Proteins
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L1 protein, Human papillomavirus type 11
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Oncogene Proteins, Viral
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Recombinant Proteins