Inhibition of tobacco mosaic virus movement by expression of an actin-binding protein

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Christina Hofmann1, Annette Niehl, Adrian Sambade

  • 1Institut de Biologie Moléculaire des Plantes du CNRS, Université de Strasbourg, 67084 Strasbourg cedex, France.

Plant Physiology
|February 17, 2009
PubMed

Insights

Tobacco mosaic virus (TMV) movement protein does not require an intact actomyosin system for cell-to-cell spread. However, actin-binding proteins can inhibit TMV movement by affecting myosin-associated trafficking.

Area of Science:

  • Plant virology
  • Cell biology
  • Molecular plant-pathogen interactions

Background:

  • Tobacco mosaic virus (TMV) cell-to-cell spread relies on its movement protein (MP).
  • MP interacts with the endoplasmic reticulum (ER) and cytoskeleton.
  • The role of actin in TMV movement has been underexplored compared to microtubules.

Purpose of the Study:

  • To investigate the role of actin filaments and myosin-dependent trafficking in TMV cell-to-cell movement.
  • To determine if TMV movement is dependent on an intact actomyosin system.

Main Methods:

  • Utilized transgenic Nicotiana benthamiana expressing Arabidopsis fimbrin's actin-binding domain (ABD2:GFP) to visualize actin dynamics and myosin-dependent Golgi trafficking.
  • Transiently expressed ABD2:GFP to inhibit actin dynamics and observed effects on TMV movement.
  • Disrupted actin networks using latrunculin B to assess TMV movement recovery.
  • Examined MP binding along actin filaments.

Main Results:

  • Transgenic plants with dynamic actin and myosin-dependent Golgi trafficking supported TMV movement.
  • Transient ABD2:GFP expression inhibited both myosin-dependent Golgi trafficking and TMV movement.
  • TMV movement was restored upon latrunculin B treatment, indicating inhibition was due to ABD2:GFP binding to actin.
  • Latrunculin B did not significantly affect TMV spread in wild-type or transgenic plants.
  • No direct binding of MP along actin filaments was observed.

Conclusions:

  • TMV cell-to-cell movement does not necessitate an intact actomyosin system.
  • Actin-binding proteins can impede TMV movement by interfering with myosin-associated protein trafficking along the ER membrane.

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