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

Biotechnol Prog. May-Jun 2003;19(3):1101-4. doi: 10.1021/bp0340077.

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

  • Comparative Study
  • Evaluation Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carrier Proteins / genetics*
  • Carrier Proteins / metabolism*
  • Gene Expression Regulation, Bacterial / genetics
  • Lactococcus lactis / genetics*
  • Lactococcus lactis / metabolism*
  • Oncogene Proteins, Viral / biosynthesis*
  • Oncogene Proteins, Viral / genetics*
  • Papillomavirus E7 Proteins
  • Protein Engineering / methods*
  • Protein Precursors / genetics
  • Protein Precursors / metabolism
  • Quality Control
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism*

Substances

  • Carrier Proteins
  • Oncogene Proteins, Viral
  • Papillomavirus E7 Proteins
  • Protein Precursors
  • Recombinant Fusion Proteins
  • oncogene protein E7, Human papillomavirus type 16