Authors:

Ethan Kaser

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About Paper:

Ralstonia solanacearum is a pathogen that causes bacterial wilt disease across numerous families. In order to induce disease, R. solanacearum uses a type-III secretion system to inject virulence proteins, also known as effectors, into the cytoplasm of the host cells. R. solanacearum injected protein 6 (Rip6) is one of over 50 effectors encoded in the R. solanacearum genome. Transient expression assays in the model plant species Nicotiana benthamiana, indicate that Rip6 localizes to the cytoskeleton and suppresses plant immune responses, including production of reactive oxygen species (ROS). The Rip6 protein does not resemble known proteins and does not have conserved protein domains. Understanding the functional domains of this effector will provide a better understanding for how this effector is able to target the cytoskeleton and suppress host immune responses. To identify the functional domains of this effector, seven truncations of the effector were generated and fused to a green fluorescent protein (GFP) tag. Using confocal microscopy, we visualized where these smaller sections are localized within the plant cell. Our results reveal that different regions of the Rip6 protein localize to distinct subcellular locations. Additionally, Rip6 truncations were tested for their immune suppression activities. Together our data suggest that different functional regions exist within the Rip6 protein.

Source:

Purdue University / 2023

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Co-authors:

Ethan Kaser