A conserved helix in C-terminal region of watermelon silver mottle virus NSs protein is imperative for protein stability affecting self-interaction, RNA silencing suppression and pathogenicity.

07:00 EST 14th January 2020 | BioPortfolio

Summary of "A conserved helix in C-terminal region of watermelon silver mottle virus NSs protein is imperative for protein stability affecting self-interaction, RNA silencing suppression and pathogenicity."

In orthotospovirus, the nonstructural NSs protein is the RNA silencing suppressor (RSS) and pathogenicity determinant. Here, we demonstrate that a putative α-helix, designated H8, spanning aa 338-369 of the C-terminal region of the NSs protein, is crucial for self-interaction of watermelon silver mottle virus (WSMoV) NSs protein and that the H8 affects RSS function. Co-immunoprecipitation, yeast two-hybrid and bimolecular fluorescence complementation analyses revealed that the triple point mutation (TPM) of H8 amino acids Y338A, H350A and F353A resulted in NSs protein self-interaction dysfunction. Transient expression of H8-deleted (ΔH8) and TPM NSs proteins in Nicotiana benthamiana plants by agroinfitration indicated that these proteins have weaker RSS activity and far less stable than wild type (WT) NSs. However, electrophoretic mobility assay revealed that siRNA binding ability of TPM NSs protein is not compromised. The pathogenicity assay of WT NSs protein expressed by the attenuated turnip mosaic virus (TuMV) vector restored severe symptoms in recombinant-infected N. benthamiana plants, but not for ΔH8 or TPM proteins. Taken together, we conclude that the H8 in the C-terminal region of NSs protein is crucial for stabilizing NSs protein through self-interaction to maintain normal functions of RSS and pathogenicity, but not for NSs-siRNA binding activity.


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This article was published in the following journal.

Name: Molecular plant-microbe interactions : MPMI
ISSN: 0894-0282


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