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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
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 .