Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2012 Feb 15:11:10.
doi: 10.1186/1475-2891-11-10.

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

Affiliations

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

Ofra Rachmaninov et al. Nutr J. .

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.

PubMed Disclaimer

Figures

Figure 1
Figure 1
Interactions (hemagglutination inhibitions and Western blots) of the seed extracts with PA-IL, PA-IIL, and CV-IIL.
Figure 2
Figure 2
PA-IL, PA-IIL, and CV-IIL interactions with human milk, quail egg white, honey, and royal jelly.
Figure 3
Figure 3
The possible structures of the active lectin-binding epitopes of the examined seed galactosylated (PA-IL-binding), mannosylated, and fucosylated (PA-IIL-binding and CV-IIL-binding) oligosaccharides. Binding sugars are marked in bold

Similar articles

Cited by

References

    1. Sadikot RT, Blackwell TS, Christman JW, Prince AS. Pathogen-host interactions in Pseudomonas aeruginosa pneumonia. Am J Respir Crit Care Med. 2005;171:1209–1223. doi: 10.1164/rccm.200408-1044SO. - DOI - PMC - PubMed
    1. Shao PL, Hsueh PR, Chang YC, Lu CY, Lee PY, Lee CY, Huang LM. Chromobacterium violaceum infection in children: A case of fatal septicemia with nasopharyngeal abscess and literature review. Pediatr Infect Dis J. 2002;21:707–709. doi: 10.1097/00006454-200207000-00022. - DOI - PubMed
    1. Gilboa-Garber N. Pseudomonas aeruginosa lectins. Methods Enzymol. 1982;83:378–385. - PubMed
    1. Zinger-Yosovich K, Sudakevitz D, Imberty A, Garber NC, Gilboa-Garber N. Production and properties of the native Chromobacterium violaceum fucose-binding lectin (CV-IIL) compared to homologous lectins of Pseudomonas aeruginosa (PA-IIL) and Ralstonia solanacearum (RS-IIL) Microbiology. 2006;152:457–463. doi: 10.1099/mic.0.28500-0. - DOI - PubMed
    1. Gilboa-Garber N, Sudakevitz D, Sheffi M, Sela R, Levene C. PA-I and PA-II lectin interactions with the ABO(H) and P blood group glycosphingolipid antigens may contribute to the broad spectrum adherence of Pseudomonas aeruginosa to human tissues in secondary infections. Glycoconj J. 1994;11:414–417. doi: 10.1007/BF00731276. - DOI - PubMed

MeSH terms

LinkOut - more resources