Soluble polymorphic bank vole prion proteins induced by co-expression of quiescin sulfhydryl oxidase in E. coli and their aggregation behaviors

Romany Abskharon, Johnny Dang, Ameer Elfarash, Zerui Wang, Pingping Shen, Lewis S. Zou, Sedky Hassan, Fei Wang, Hisashi Fujioka, Jan Steyaert, Mentor Mulaj, Witold K. Surewicz, Joaquín Castilla, Alexandre Wohlkonig*, Wen Quan Zou

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)


Background: The infectious prion protein (PrPSc or prion) is derived from its cellular form (PrPC) through a conformational transition in animal and human prion diseases. Studies have shown that the interspecies conversion of PrPC to PrPSc is largely swayed by species barriers, which is mainly deciphered by the sequence and conformation of the proteins among species. However, the bank vole PrPC (BVPrP) is highly susceptible to PrPSc from different species. Transgenic mice expressing BVPrP with the polymorphic isoleucine (109I) but methionine (109M) at residue 109 spontaneously develop prion disease. Results: To explore the mechanism underlying the unique susceptibility and convertibility, we generated soluble BVPrP by co-expression of BVPrP with Quiescin sulfhydryl oxidase (QSOX) in Escherichia coli. Interestingly, rBVPrP-109M and rBVPrP-109I exhibited distinct seeded aggregation pathways and aggregate morphologies upon seeding of mouse recombinant PrP fibrils, as monitored by thioflavin T fluorescence and electron microscopy. Moreover, they displayed different aggregation behaviors induced by seeding of hamster and mouse prion strains under real-time quaking-induced conversion. Conclusions: Our results suggest that QSOX facilitates the formation of soluble prion protein and provide further evidence that the polymorphism at residue 109 of QSOX-induced BVPrP may be a determinant in mediating its distinct convertibility and susceptibility.

Original languageEnglish
Article number170
JournalMicrobial Cell Factories
Issue number1
Publication statusPublished - Oct 4 2017
Externally publishedYes


  • Aggregation
  • Bank vole
  • Circular dichroism
  • Electron microscopy
  • Prion diseases
  • Prion protein
  • Prions
  • Quiescin sulfhydryl oxidase (QSOX)
  • Surface plasmon resonance (SPR)
  • Thioflavin T (ThT)

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology


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