Analysis of Positional and Structural Variations of the Adhesion-Related Protein P89 in Various Spiroplasma citri Strains


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Derecik K., Tulum I., Çağlayan K.

Uluslararası Katılımlı IX. Bitki Koruma Kongresine, Ankara, Turkey, 3 - 05 September 2025, pp.58, (Summary Text)

  • Publication Type: Conference Paper / Summary Text
  • City: Ankara
  • Country: Turkey
  • Page Numbers: pp.58
  • Hatay Mustafa Kemal University Affiliated: Yes

Abstract

Spiroplasma citri are Gram-positive bacteria with motile helical cells that lack a cell wall. S. citri is recognized as the pathogen of Citrus Stubborn Disease and horseradish brittle root disease, but it can also cause diseases of carrots, sesame and various ornamentals and weeds. In the Mediterranean region, this intracellular pathogen is spread from plant to plant by the leafhopper vector Circulifer haematoceps. The successful spread of S. citri depends on the mediation of receptor-ligand interactions by S. citri adhesins and the crossing of the intestinal epithelium and salivary gland barrier by endocytosis from the insect haemocoel. P89 (SARP1), one of the two adhesin proteins thought to be responsible for adhesion and invasion in host cells in terms of spiroplasma-host interaction, was analyzed in detail by sequence and structure in this study. P89 homologs were investigated in the genomes of S. citri strains that had been cultured for many years and were obtained from various plants and insects in our recent field studies. Their distribution in the genome and plasmids was examined, and the differences between orthologs and paralogs were determined at the sequence level. It was observed that in some culture samples, P89 genes lost their plasmid positioning, integrated into the chromosome and transformed into pseudogenes, unlike in recently collected insect and plant strains. Using the amino acid sequences of P89 homologues, 3D protein models were constructed by using AlphaFold 3 application and it was determined that P89 homologues showed a multi-domain protein structure in which beta-propeller, beta-sandwich, ubiquitin-like and spiralin-like domains were connected to each other sequentially. Various structural variations were also observed between the domains of P89 homologues in the strains we examined and the possible effects of these variations on spiroplasma-host interactions were examined. The results obtained in this study will provide a model for how different S. citri strains invade host cells and cross cellular barriers in terms of spiroplasma-host interactions.

 

Keywords: Spiroplasma, P89, adhesin, host interaction