Scientific Reports · 2021 · 30 citations · 41 references
Life SciencesEntomologyMicrobiologyCell AdhesionInsect ImmunologyInsect PhysiologyAdhesion MoleculesInsect ExoskeletonInsect PathogensVector-host InteractionsLectin InteractionsLectin RecognitionLectin-carbohydrate InteractionsLectin-carbohydrate RecognitionLectin-glycan RecognitionLectin-mediated AttachmentLectin-mediated Microbial InteractionsLectins
The flavescence dorée phytoplasma undergoes a propagative cycle in its insect vectors by first interacting with the insect cell surfaces, primarily in the midgut lumen and subsequently in the salivary glands. Adhesion of flavescence dorée phytoplasma to insect cells is mediated by the adhesin VmpA. We hypothesize that VmpA may have lectin-like activity, similar to several adhesins of bacteria that invade the insect gut. We first demonstrated that the luminal surface of the midgut and the basal surface of the salivary gland cells of the natural vector Scaphoideus titanus and those of the experimental vector Euscelidius variegatus were differentially glycosylated. Using ELISA, inhibition and competitive adhesion assays, and protein overlay assays in the Euva-6 insect cell line, we showed that the protein VmpA binds insect proteins in a lectin-like manner. In conclusion, the results of this study indicate that N-acetylglucosamine and mannose present on the surfaces of the midgut and salivary glands serve as recognition sites for the phytoplasma adhesin VmpA.
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Trimeric structure of a C-type mannose-binding protein
William I. Weis, Kurt Drickamer · Structure · 1994 · 313 citations · Full text
Shiho Suzuki, Kenro Oshima, Shigeyuki Kakizawa et al. · Proceedings of the National Academy of Sciences · 2006 · 205 citations · Full text
Elisa Angelini, D. Clair, M. Borgo et al. · Federal Research Centre for Cultivated Plants (Julius Kühn-Institut) · 2015 · 182 citations · Full text