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Characterization of membrane association of Rinderpest virus matrix protein

R Subhashri1, M S Shaila

  • 1Department of Microbiology and Cell biology, Indian Institute of Science, Bangalore, Karnataka 560012, India.

Biochemical and Biophysical Research Communications
|March 6, 2007
PubMed

Insights

Rinderpest virus matrix (M) protein associates with the host cell membrane, behaving like an integral membrane protein. This finding is crucial for understanding paramyxovirus assembly and maturation.

Area of Science:

  • Virology
  • Cell Biology
  • Molecular Biology

Background:

  • Paramyxovirus matrix proteins are essential for viral assembly and maturation.
  • Enveloped virus matrix proteins often exhibit intrinsic membrane association capabilities.

Purpose of the Study:

  • To characterize the membrane association of the Rinderpest virus matrix (M) protein.
  • To understand the M protein's role in viral particle formation.

Main Methods:

  • Expression of Rinderpest virus M protein in host cells.
  • Localization studies using GFP fusion protein.
  • Assays under high salt and alkaline conditions to assess membrane dissociation.

Main Results:

  • Rinderpest virus M protein localizes to both the cytoplasm and plasma membrane when expressed alone.
  • GFP-tagged M protein accumulates in plasma membrane protrusions.
  • M protein shows partial dissociation from the cell membrane under high salt and alkaline stress.

Conclusions:

  • Rinderpest virus M protein exhibits characteristics of an integral membrane protein.
  • Despite its primary structure suggesting peripheral association, M protein's behavior indicates stronger membrane integration.
  • This behavior is significant for understanding the mechanisms of Rinderpest virus assembly.

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