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Interrogating the Dimerization Interface of the Prion Protein Via Site-Specific Mutations to

Sudheer Babu Sangeetham1, Krisztina Huszár2, Petra Bencsura2

  • 1Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.

Journal of Molecular Biology
|May 21, 2018
PubMed

Insights

Researchers investigated prion protein (PrP) oligomerization, a key process in transmissible spongiform encephalopathies. They identified specific regions of the N-terminal part of the mouse prion protein (mPrP) as crucial for dimer formation during this process.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Neuroscience

Background:

  • Transmissible spongiform encephalopathies (TSEs) involve prion protein (PrP) misfolding from helical monomers to beta-sheet-rich aggregates.
  • The exact mechanism of infectious and toxic oligomer formation from PrP monomers remains unclear.

Purpose of the Study:

  • To investigate the structural basis of prion protein dimer formation, a potential intermediate in oligomerization.
  • To identify the specific regions of the prion protein involved in dimer interfaces.

Main Methods:

  • Creation of 25 mouse prion protein (mPrP) variants with site-specifically incorporated para-benzoyl-phenylalanine (pBpa), a cross-linkable non-natural amino acid.
  • Utilizing pBpa cross-linking to probe the dimer interface of mPrP.

Main Results:

  • The N-terminal region of the prion protein, particularly residues near positions 127 and 107, is integral to the dimer interface.
  • These findings provide insights into the initial steps of PrP oligomerization.

Conclusions:

  • The N-terminal regions of mPrP are critical for forming dimers, a likely step in prion protein aggregation.
  • pBpa-containing mPrP variants offer a valuable tool for further structural studies of pathogenic PrP species.
Keywords:
DimerizationPhoto-crosslinkingPrionProtein conformational stabilitypBpa

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