Preventing Pseudomonas aeruginosa and Chromobacterium violaceum infections by anti-adhesion-active components of edible seeds

<p>Abstract</p> <p>Background</p> <p><it>Pseudomonas aeruginosa </it>adhesion to animal/human cells for infection establishment involves adhesive proteins, including its galactose- and fucose-binding lectins PA-IL (LecA) and PA-IIL (LecB). The lectin binding to the target-cell receptors may be blocked by compatible glycans that compete with those of the receptors, functioning as anti-adhesion glycodecoys. The anti-adhesion treatment is of the utmost importance for abrogating devastating antibiotic-resistant <it>P. aeruginosa </it>infections in immunodeficient and cystic fibrosis (CF) patients. This strategy functions in nature in protecting embryos and neonates. We have shown that PA-IL, PA-IIL, and also CV-IIL (a PA-IIL homolog produced in the related pathogen <it>Chromobacterium violaceum</it>) are highly useful for revealing natural glycodecoys that surround embryos in diverse avian eggs and are supplied to neonates in milks and royal jelly. In the present study, these lectins were used as probes to search for seed embryo-protecting glycodecoys.</p> <p>Methods</p> <p>The lectin-blocking glycodecoy activities were shown by the hemagglutination-inhibition test. Lectin-binding glycoproteins were detected by Western blotting with peroxidase-labeled lectins.</p> <p>Results</p> <p>The present work reports the finding - by using PA-IL, PA-IIL, and CV-IIL - of rich glycodecoy activities of low (< 10 KDa) and high MW (> 10 kDa) compounds (including glycoproteins) in extracts of cashew, cocoa, coffee, pumpkin, and tomato seeds, resembling those of avian egg whites, mammal milks, and royal jelly.</p> <p>Conclusions</p> <p>Edible seed extracts possess lectin-blocking glycodecoys that might protect their embryos from infections and also might be useful for hampering human and animal infections.</p

Production and properties of the native <i>Chromobacterium violaceum</i> fucose-binding lectin (CV-IIL) compared to homologous lectins of <i>Pseudomonas aeruginosa</i> (PA-IIL) and <i>Ralstonia solanacearum</i> (RS-IIL)

International audienc

The five bacterial lectins (PA-IL, PA-IIL, RSL, RS-IIL, and CV-IIL): Interactions with diverse animal cells and glycoproteins

International audienc