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Peptide-based Identification of Functional Motifs and their Binding Partners
14:28

Peptide-based Identification of Functional Motifs and their Binding Partners

Published on: June 30, 2013

Mutation of YMYL in the Nipah virus matrix protein abrogates budding and alters subcellular localization

Michael J Ciancanelli1, Christopher F Basler

  • 1Department of Microbiology, Box 1124, Mount Sinai School of Medicine, 1 Gustave L. Levy Place, New York, NY 10029, USA.

Journal of Virology
|September 29, 2006
PubMed

Insights

Nipah virus matrix (M) protein budding was studied. A YMYL sequence was found to be crucial for virus-like particle release, acting as a late domain.

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • Matrix (M) proteins are essential for paramyxovirus budding.
  • Nipah virus (NiV) is an emerging, highly lethal paramyxovirus requiring assembly process characterization.

Purpose of the Study:

  • To investigate the assembly and budding mechanism of the Nipah virus matrix (M) protein.
  • To identify functional domains within the NiV M protein involved in viral egress.

Main Methods:

  • Expression of NiV M protein to form virus-like particles (VLPs).
  • Site-directed mutagenesis of a putative late domain (YMYL) in NiV M.
  • Complementation assays using Ebola virus VP40 matrix protein.

Main Results:

  • NiV M expression alone produced VLPs resembling NiV.
  • Mutation of the YMYL sequence abolished VLP release and caused M protein nuclear relocalization.
  • The YMYL sequence restored budding when fused to a mutant Ebola virus VP40 protein.

Conclusions:

  • The YMYL sequence in NiV M functions as a critical late domain for viral budding.
  • This sequence likely acts as a trafficking signal directing M protein to the plasma membrane for egress.
  • Understanding NiV M's role in budding is crucial for developing antiviral strategies.

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