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Fusion to a carrier protein and a synthetic propeptide enhances E7 HPV-16 production and secretion in Lactococcus lactis

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Bermudez Humaran, Luis, L. | Cortes-Perez, Naima | Le Loir, Yves | Gruss, Alexandra, A. | Rodríguez-Padilla, Cristina | Saucedo-Cardenas, Odila | Langella, Philippe, P. | Montes de Oca-Luna, Roberto

Edité par CCSD ; Wiley -

International audience. 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.

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