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Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods
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Hsp72 recognizes a P binding motif in the measles virus N protein C-terminus

Xinsheng Zhang1, Jean-Marie Bourhis, Sonia Longhi

  • 1Department of Veterinary Biosciences, The Ohio State University, Columbus, 43210, USA.

Virology
|May 26, 2005
PubMed

Insights

The heat shock protein hsp72 binds measles virus nucleocapsids via Box-2 of the N protein, not Box-3. This interaction competitively inhibits viral polymerase binding, suggesting a host mechanism to control measles virus gene expression.

Area of Science:

  • Virology
  • Molecular Biology
  • Immunology

Background:

  • The 70-kDa heat shock protein (hsp72) interacts with measles virus (MV) nucleocapsids, enhancing viral gene expression.
  • The MV N protein's cytoplasmic tail (N(TAIL)) has hydrophobic domains (Box-1-3) potentially mediating hsp72 binding.

Purpose of the Study:

  • To elucidate the specific binding sites and mechanisms of hsp72 interaction with the MV N protein.
  • To investigate the functional consequences of hsp72 binding on MV gene expression and replication.

Main Methods:

  • Site-directed mutagenesis of N(TAIL) hydrophobic domains (Box-1-3).
  • Analysis of hsp72-nucleocapsid complex formation using virus deficient in specific Box interactions.
  • Assessment of competitive binding between hsp72 and the viral P protein X domain (XD).

Main Results:

  • Virus deficient in Box-3/hsp72 interaction still forms nucleocapsid/hsp72 complexes.
  • Box-2, not Box-1, was identified as the primary mediator of high-affinity hsp72 binding to N(TAIL).
  • hsp72 competitively inhibits the binding of the viral P protein XD to N(TAIL) Box-2.

Conclusions:

  • hsp72 binds measles virus nucleocapsids with high affinity via Box-2 of the N protein.
  • This interaction represents a potential host-mediated regulatory mechanism by interfering with viral polymerase complex formation.
  • The findings reveal a novel interplay between a host heat shock protein and viral replication machinery.

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