Abstract
An inducible system to improve and stabilize the production of an extremely labile protein (E7 antigen of human papillomavirus type 16) was developed in the food-grade bacterium Lactococcus lactis. A protein carrier, the staphylococcal nuclease Nuc, was fused either to N- or C-termini of E7 protein, and the resulting hybrid proteins were rescued from intracellular proteolysis but poorly secreted by L. lactis. A synthetic propeptide (LEISSTCDA) was then fused and significantly improved the secretion efficiency of the hybrid protein Nuc-E7 by L. lactis.
Publication types
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Comparative Study
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Evaluation Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Carrier Proteins / genetics*
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Carrier Proteins / metabolism*
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Gene Expression Regulation, Bacterial / genetics
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Lactococcus lactis / genetics*
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Lactococcus lactis / metabolism*
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Oncogene Proteins, Viral / biosynthesis*
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Oncogene Proteins, Viral / genetics*
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Papillomavirus E7 Proteins
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Protein Engineering / methods*
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Protein Precursors / genetics
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Protein Precursors / metabolism
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Quality Control
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism*
Substances
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Carrier Proteins
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Oncogene Proteins, Viral
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Papillomavirus E7 Proteins
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Protein Precursors
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Recombinant Fusion Proteins
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oncogene protein E7, Human papillomavirus type 16