title: Preventing Pseudomonas aeruginosa and Chromobacterium violaceum infections by anti-adhesion-active components of edible seeds.
abstract: BACKGROUND
  Pseudomonas aeruginosa 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 P. aeruginosa 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 Chromobacterium violaceum) 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.
  
  
  METHODS
  The lectin-blocking glycodecoy activities were shown by the hemagglutination-inhibition test. Lectin-binding glycoproteins were detected by Western blotting with peroxidase-labeled lectins.
  
  
  RESULTS
  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.
  
  
  CONCLUSIONS
  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.
authors.affiliation: The Mina & Everard Goodman Faculty of Life Sciences, Bar-Ilan University, Ramat-Gan, Israel.
authors.forename: Ofra
authors.initials: O
authors.lastname: Rachmaninov
authors.forename: Keren D
authors.initials: KD
authors.lastname: Zinger-Yosovich
authors.forename: Nechama
authors.initials: N
authors.lastname: Gilboa-Garber
mesh_terms: D018829:Adhesins, Bacterial / Q000378:metabolism*; D031021:Anacardium / Q000737:chemistry; D000818:Animals; D001422:Bacterial Adhesion / Q000187:drug effects*; D015153:Blotting, Western; D002099:Cacao / Q000737:chemistry; D002861:Chromobacterium / Q000187:drug effects / Q000254:growth & development; D003069:Coffee / Q000737:chemistry; D004529:Egg White / Q000737:chemistry; D005227:Fatty Acids / Q000737:chemistry; D005690:Galactose / Q000378:metabolism; D006023:Glycoproteins / Q000032:analysis / Q000378:metabolism; D006385:Hemagglutination Inhibition Tests; D037102:Lectins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D018551:Solanum lycopersicum / Q000737:chemistry; D008892:Milk / Q000737:chemistry; D010936:Plant Extracts / Q000494:pharmacology*; D011485:Protein Binding; D011552:Pseudomonas Infections / Q000517:prevention & control*; D011550:Pseudomonas aeruginosa / Q000187:drug effects / Q000254:growth & development; D012639:Seeds / Q000737:chemistry*; D000099219:Royal Jelly
chemical_list: D018829:Adhesins, Bacterial; D003069:Coffee; D005227:Fatty Acids; D005690:Galactose; D006023:Glycoproteins; D037102:Lectins; D010936:Plant Extracts; D000099219:Royal Jelly; C102929:LecA protein, bacteria; C534600:LecB protein, Pseudomonas aeruginosa; C038692:adhesin, Pseudomonas; C027112:fucose-binding lectin