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Fusion to a Carrier Protein and a Synthetic Propeptide Enhances E7 HPV‐16 Production and Secretion in Lactococcus lactis
Author(s) -
BermúdezHumarán Luis G.,
CortesPerez Naima G.,
Loir Yves Le,
Gruss Alexandra,
RodriguezPadilla Cristina,
SaucedoCardenas Odila,
Langella Philippe,
Montes de OcaLuna Roberto
Publication year - 2003
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp0340077
Subject(s) - lactococcus lactis , secretion , protein precursor , proteolysis , chemistry , protein biosynthesis , secretory protein , fusion protein , intracellular , nuclease , bacteria , biochemistry , biology , microbiology and biotechnology , recombinant dna , enzyme , gene , lactic acid , genetics
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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