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• W2099164892 abstract "Geminivirus AL2 and L2 proteins cause enhanced susceptibility, characterized primarily by an increase in viral infectivity, when expressed in transgenic plants. Here, we present genetic and biochemical evidence that enhanced susceptibility is attributable to the interaction of AL2 and L2 with SNF1 kinase, a global regulator of metabolism. Specifically, we show that AL2 and L2 inactivate SNF1 in vitro and in vivo. We further demonstrate that expression of an antisense SNF1 transgene in Nicotiana benthamiana plants causes enhanced susceptibility similar to that conditioned by the AL2 and L2 transgenes, whereas SNF1 overexpression leads to enhanced resistance. Transgenic plants expressing an AL2 protein that lacks a significant portion of the SNF1 interaction domain do not display enhanced susceptibility. Together, these observations suggest that the metabolic alterations mediated by SNF1 are a component of innate antiviral defenses and that SNF1 inactivation by AL2 and L2 is a counterdefensive measure. They also indicate that geminiviruses are able to modify host metabolism to their own advantage, and they provide a molecular link between metabolic status and inherent susceptibility to viral pathogens." @default.
• W2099164892 created "2016-06-24" @default.
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• W2099164892 date "2003-03-04" @default.
• W2099164892 modified "2023-10-09" @default.
• W2099164892 title "Geminivirus AL2 and L2 Proteins Interact with and Inactivate SNF1 Kinase" @default.
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• W2099164892 doi "https://doi.org/10.1105/tpc.009530" @default.
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