A high-performance thioredoxin-based scaffold for peptide immunogen construction: Proof-of-concept testing with a human papillomavirus epitope

Elena Canali, Angelo Bolchi, Gloria Spagnoli, Hanna Seitz, Ivonne Rubio, Thelma A. Pertinhez, Martin Müller, Simone Ottonello

Research output: Contribution to journalArticle

Abstract

Escherichia coli thioredoxin has been previously exploited as a scaffold for the presentation/stabilization of peptide aptamers as well as to confer immunogenicity to peptide epitopes. Here we focused on other key features of thioredoxin that are of general interest for the production of safer and more effective peptide immunogens, such as a high thermal stability, lack of cross-reactivity and a low-cost of production. We identified thioredoxin from the archaebacterium Pyrococcus furiosus (PfTrx) as a novel scaffold meeting all the above criteria. PfTrx is a highly thermostable and protease-resistant scaffold with a strong (poly)peptide solubilisation capacity. Anti-PfTrx antibodies did not cross-react with mouse, nor human thioredoxin. Untagged PfTrx bearing a previously identified HPV16-L2 peptide epitope was obtained in a >90% pure form with a one-step thermal purification procedure and effectively elicited the production of neutralizing anti-HPV antibodies. We thus propose PfTrx as a superior, general-purpose scaffold for the construction of safe, stable, and low-cost peptide immunogens.

Original languageEnglish
Article number4729
JournalScientific Reports
Volume4
DOIs
Publication statusPublished - Apr 22 2014

ASJC Scopus subject areas

  • General
  • Medicine(all)

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    Canali, E., Bolchi, A., Spagnoli, G., Seitz, H., Rubio, I., Pertinhez, T. A., Müller, M., & Ottonello, S. (2014). A high-performance thioredoxin-based scaffold for peptide immunogen construction: Proof-of-concept testing with a human papillomavirus epitope. Scientific Reports, 4, [4729]. https://doi.org/10.1038/srep04729