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Characterization of a slow-migrating component of the rabies virus matrix protein strongly associated with the viral

Tomomi Nakahara1, Harufusa Toriumi, Takashi Irie

  • 1Department of Molecular Microbiology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan.

Microbiology and Immunology
|December 26, 2003
PubMed

Insights

Rabies virus matrix (M) protein exists as monomers and a 54-kDa homodimer. This M protein homodimer strongly associates with the viral glycoprotein (G), influencing its conformation and potential membrane interactions.

Area of Science:

  • Virology
  • Molecular Biology
  • Protein Biochemistry

Background:

  • The rabies virus matrix (M) protein is crucial for viral assembly and structure.
  • Understanding M protein's various forms and interactions is key to deciphering viral pathogenesis.

Purpose of the Study:

  • To characterize the different molecular forms of rabies virus M protein.
  • To investigate the interactions of M protein forms with other viral components, particularly the glycoprotein (G).

Main Methods:

  • Non-reducing and two-dimensional (2-D) gel electrophoresis to analyze M protein forms.
  • Sodium deoxycholate and nonionic detergent extraction to assess solubility.
  • Monoclonal antibody (mAb) precipitation assays to study M protein-G interactions.

Main Results:

  • Identified monomeric (23- and 24-kDa) and a minor 54-kDa M protein band in virions and infected cells.
  • The 54-kDa M protein component, present at 20-30% in virions, showed distinct extraction properties and was efficiently precipitated by an N-terminal specific mAb.
  • This mAb coprecipitated the viral glycoprotein (G), indicating a strong association between the 54-kDa M protein and G.

Conclusions:

  • The 54-kDa M protein species is a homodimer with an N-terminal exposed conformation.
  • This M protein homodimer exhibits strong association with the rabies virus glycoprotein (G).
  • The findings suggest potential roles in viral structure, assembly, and membrane association.

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