Location: Molecular Plant Pathology Laboratory
Title: Lectin binding assay reveals phytoplasma infection-induced alteration of plant host protein glycosylationAuthor
|
Submitted to: Phytopathogenic Mollicutes
Publication Type: Peer Reviewed Journal Publication Acceptance Date: 4/4/2023 Publication Date: 5/23/2023 Citation: Kim, B., Inaba, J., Zhao, Y., Wei, W. 2023. Lectin binding assay reveals phytoplasma infection-induced alteration of plant host protein glycosylation. Phytopathogenic Mollicutes. 13(1):7-8. https://doi.org/10.5958/2249-4677.2023.00004.X. DOI: https://doi.org/10.5958/2249-4677.2023.00004.X Interpretive Summary: Phytoplasmas are plant pathogenic bacteria responsible for numerous diseases in agriculturally important crops. Phytoplasma infection can change many aspects of the biochemical and physiological processes in host plants. Glycosylation is a common posttranslational modification that contributes to the activity and stability of diverse eukaryotic proteins. Using a lectin binding assay, ARS scientists at the Beltsville Agriculture Research Center investigated whether phytoplasma infection can alter protein glycosylation profiles in susceptible plants. Results from the study revealed that, in potato purple top phytoplasma-infected tomato plants, the levels of protein glycosylation involving mannose, galactose, and N-galactosamine glycans were increased, while those involving fucose glycans were decreased. Confocal microscopic images indicated that the altered glycosylation activities occurred mainly in the phloem tissue of infected plants. The findings will help elucidate the role of protein glycosylation in phytoplasma pathogenesis and host defense response. This article will be of interest to research scientists who are studying pathogen-host interactions and molecular basis of phytoplasma diseases. Technical Abstract: Glycosylation is a common posttranslational modification that contributes to the activity and stability of diverse eukaryotic proteins. The present study performed a lectin binding assay using four biotinylated lectins and investigated changes in protein glycosylation patterns in tomato plants infected with potato purple top (PPT) phytoplasma. The results revealed that in PPT phytoplasma-infected tomato plants, there was an increase in the levels of protein glycosylation involving mannose, galactose, and N-galactosamine glycans, while those involving fucose glycans were decreased. Confocal microscopy analysis indicated that the altered glycosylation activities occurred mainly in the phloem tissue of infected plants. These findings suggest that PPT phytoplasma infection can significantly impact the glycosylation patterns of tomato plant proteins, which could provide valuable insights into the mechanisms of plant response to phytoplasma infection and potential strategies for crop protection. |
