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Measles virus matrix protein is not cotransported with the viral glycoproteins but requires virus infection for

Petra Riedl1, Markus Moll, Hans-Dieter Klenk

  • 1Institute of Virology, Philipps University of Marburg, Robert-Koch-Strasse 17, 35037 Marburg, Germany.

Virus Research
|February 28, 2002
PubMed

Insights

Measles virus (MV) matrix protein (M) independently targets the apical membrane, unlike viral glycoproteins. M protein binds membranes intrinsically but requires MV infection for surface transport.

Area of Science:

  • Virology
  • Cell Biology
  • Molecular Biology

Background:

  • Measles virus (MV) glycoproteins H and F localize to both apical and basolateral membranes of polarized cells.
  • The MV matrix protein (M) shows selective apical accumulation, distinct from glycoprotein localization.

Purpose of the Study:

  • To investigate the subcellular transport mechanism of the measles virus matrix protein (M).
  • To determine if M protein requires viral glycoproteins for surface transport.
  • To elucidate the intrinsic properties of M protein governing its membrane association.

Main Methods:

  • Analysis of MV-infected polarized Madin-Darby canine kidney cells.
  • Monensin treatment to disrupt Golgi transport.
  • Expression of M protein in the absence of other viral proteins.
  • Flotation analysis to assess M protein's association with cellular membranes.

Main Results:

  • MV matrix protein (M) accumulates selectively at the apical plasma membrane, independent of glycoproteins.
  • M protein demonstrates an intrinsic ability to bind to cellular lipid membranes.
  • M protein transport to the plasma membrane necessitates a factor present only in MV-infected cells, not solely glycoproteins.

Conclusions:

  • The measles virus matrix protein (M) utilizes a unique, independent pathway for apical surface transport.
  • M protein's intrinsic membrane-binding capacity is crucial but insufficient for surface delivery.
  • Viral context, beyond glycoproteins, is essential for M protein's final destination at the plasma membrane.

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