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Updated: Mar 6, 2026

Engineering Antiviral Agents via Surface Plasmon Resonance
Published on: June 14, 2022
Antiviral Resistance Protein Tm-22 Functions on the Plasma Membrane
Tianyuan Chen1,2,3, Dan Liu1,2,3, Xiaolin Niu1,2,3
1Center for Plant Biology, Tsinghua-Peking Joint Center for Life Sciences, MOE Key Laboratory of Bioinformatics, School of Life Sciences, Tsinghua University, Beijing 100084, China (T.C., D.L., X.N., J.W., L.Q., L.H., N.L., J.Z., Y.L.).
Abstract:
The tomato Tobacco mosaic virus resistance-2 (Tm-2 ) gene encodes a coiled-coil-nucleotide binding site-Leu-rich repeat protein lacking a conventional plasma membrane (PM) localization motif. Tm-22 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-22 functions is unclear. Here, we demonstrate that Tm-22 interacts with TMV MP to form a protein complex at the PM We show that both inactive and active Tm-22 proteins are localized to the PM When restricted to PM by fusing Tm-22 to the S-acylated PM association motif, the Tm-22 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-22 function. These results suggest that Tm-22-mediated resistance takes place on PM without requirement of its Avr protein to be located to PD.
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