4.8 Article

Antiviral Resistance Protein Tm-22 Functions on the Plasma Membrane

Journal

PLANT PHYSIOLOGY
Volume 173, Issue 4, Pages 2399-2410

Publisher

OXFORD UNIV PRESS INC
DOI: 10.1104/pp.16.01512

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Funding

  1. National Natural Science Foundation of China [31530059, 31421001, 31470254, 31300134, 31370180]
  2. National Basic Research Program of China [2014CB138400]
  3. National Transgenic Program of China [2016ZX08009-003-001, 2016ZX08009001-004]

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The tomato Tobacco mosaic virus resistance-2(2) (Tm-2(2)) gene encodes a coiled-coil-nucleotide binding site-Leu-rich repeat protein lacking a conventional plasma membrane (PM) localization motif. Tm-2(2) confers plant extreme resistance against tobamoviruses including Tobacco mosaic virus (TMV) by recognizing the avirulence (Avr) viral movement protein (MP). However, the subcellular compartment where Tm-2(2) functions is unclear. Here, we demonstrate that Tm-2(2) interacts with TMV MP to form a protein complex at the PM. We show that both inactive and active Tm-2(2) proteins are localized to the PM. When restricted to PM by fusing Tm-2(2) to the S-acylated PM association motif, the Tm-2(2) fusion protein can still induce a hypersensitive response cell death, consistent with its activation at the PM. Through analyses of viral MP mutants, we find that the plasmodesmata (PD) localization of the Avr protein MP is not required for Tm-2(2) function. These results suggest that Tm-2(2)-mediated resistance takes place on PM without requirement of its Avr protein to be located to PD.

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