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Spiroplasma citri Surface Protein P89 Implicated in Adhesion to Cells of the Vector Circulifer tenellus

J Yu, A C Wayadande, J Fletcher

    Phytopathology
    |October 24, 2008
    PubMed

    Insights

    A key surface protein (P89) on Spiroplasma citri facilitates its attachment to its leafhopper vector, Circulifer tenellus. Removing this protein prevents adherence, while its regeneration restores the pathogen's ability to attach.

    Area of Science:

    • Plant Pathology
    • Microbiology
    • Insect Vector Biology

    Background:

    • Spiroplasma citri is a plant-pathogenic mollicute.
    • Understanding pathogen adherence to insect vectors is crucial for disease transmission.

    Purpose of the Study:

    • To investigate the molecular mechanisms of Spiroplasma citri adherence to its vector, Circulifer tenellus.
    • To identify specific spiroplasma surface components involved in this interaction.

    Main Methods:

    • Development of two microtiter plate assays to quantify adherence.
    • Protease treatment (proteinase K, pronase) of spiroplasmas.
    • Electrophoresis, western blotting, and Triton X-114 phase partitioning of spiroplasma membrane proteins.
    • Regeneration experiments following protease treatment.

    Main Results:

    • Spiroplasma citri adherence to Circulifer tenellus cells was significantly reduced by proteinase K or pronase treatment.
    • Protease treatment decreased the intensity of a major 89 kDa membrane protein (P89) and a 46 kDa polypeptide (P46).
    • P89 regeneration restored the pathogen's attachment capability, suggesting P89 mediates adherence.

    Conclusions:

    • The spiroplasma surface protein P89 plays a critical role in the adherence of Spiroplasma citri to its leafhopper vector, Circulifer tenellus.
    • This protein-mediated interaction is essential for the pathogen's attachment to its vector cells.

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