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GalNAc/Gal-binding Rhizoctonia solani agglutinin has antiproliferative activity in Drosophila melanogaster S2 cells via MAPK and JAK/STAT signaling

Mohamad Hamshou UGent, Els Van Damme UGent, Gianni Vandenborre UGent, Bart Ghesquière UGent, Geert Trooskens UGent, Kris Gevaert UGent and Guy Smagghe UGent (2012) PLOS ONE. 7(4).
abstract
Rhizoctonia solani agglutinin, further referred to as RSA, is a lectin isolated from the plant pathogenic fungus Rhizoctonia solani. Previously, we reported a high entomotoxic activity of RSA towards the cotton leafworm Spodoptera littoralis. To better understand the mechanism of action of RSA, Drosophila melanogaster Schneider S2 cells were treated with different concentrations of the lectin and FITC-labeled RSA binding was examined using confocal fluorescence microscopy. RSA has antiproliferative activity with a median effect concentration (EC50) of 0.35 mu M. In addition, the lectin was typically bound to the cell surface but not internalized. In contrast, the N-acetylglucosamine-binding lectin WGA and the galactose-binding lectin PNA, which were both also inhibitory for S2 cell proliferation, were internalized whereas the mannose-binding lectin GNA did not show any activity on these cells, although it was internalized. Extracted DNA and nuclei from S2 cells treated with RSA were not different from untreated cells, confirming inhibition of proliferation without apoptosis. Pre-incubation of RSA with N-acetylgalactosamine clearly inhibited the antiproliferative activity by RSA in S2 cells, demonstrating the importance of carbohydrate binding. Similarly, the use of MEK and JAK inhibitors reduced the activity of RSA. Finally, RSA affinity chromatography of membrane proteins from S2 cells allowed the identification of several cell surface receptors involved in both signaling transduction pathways.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
TRANSDUCTION PATHWAY, TYROSINE KINASE, FUNGAL LECTIN, PROTEIN, LINES, ACTIVATION
journal title
PLOS ONE
PLoS One
volume
7
issue
4
article_number
e33680
pages
10 pages
Web of Science type
Article
Web of Science id
000305350600005
JCR category
MULTIDISCIPLINARY SCIENCES
JCR impact factor
3.73 (2012)
JCR rank
7/56 (2012)
JCR quartile
1 (2012)
ISSN
1932-6203
DOI
10.1371/journal.pone.0033680
project
Center for nano- and biophotonics (NB-Photonics)
language
English
UGent publication?
yes
classification
A1
copyright statement
I have retained and own the full copyright for this publication
id
2038039
handle
http://hdl.handle.net/1854/LU-2038039
date created
2012-02-17 17:11:42
date last changed
2014-05-26 09:50:50
@article{2038039,
  abstract     = {Rhizoctonia solani agglutinin, further referred to as RSA, is a lectin isolated from the plant pathogenic fungus Rhizoctonia solani. Previously, we reported a high entomotoxic activity of RSA towards the cotton leafworm Spodoptera littoralis. To better understand the mechanism of action of RSA, Drosophila melanogaster Schneider S2 cells were treated with different concentrations of the lectin and FITC-labeled RSA binding was examined using confocal fluorescence microscopy. RSA has antiproliferative activity with a median effect concentration (EC50) of 0.35 mu M. In addition, the lectin was typically bound to the cell surface but not internalized. In contrast, the N-acetylglucosamine-binding lectin WGA and the galactose-binding lectin PNA, which were both also inhibitory for S2 cell proliferation, were internalized whereas the mannose-binding lectin GNA did not show any activity on these cells, although it was internalized. Extracted DNA and nuclei from S2 cells treated with RSA were not different from untreated cells, confirming inhibition of proliferation without apoptosis. Pre-incubation of RSA with N-acetylgalactosamine clearly inhibited the antiproliferative activity by RSA in S2 cells, demonstrating the importance of carbohydrate binding. Similarly, the use of MEK and JAK inhibitors reduced the activity of RSA. Finally, RSA affinity chromatography of membrane proteins from S2 cells allowed the identification of several cell surface receptors involved in both signaling transduction pathways.},
  articleno    = {e33680},
  author       = {Hamshou, Mohamad and Van Damme, Els and Vandenborre, Gianni and Ghesqui{\`e}re, Bart and Trooskens, Geert and Gevaert, Kris and Smagghe, Guy},
  issn         = {1932-6203},
  journal      = {PLOS ONE},
  keyword      = {TRANSDUCTION PATHWAY,TYROSINE KINASE,FUNGAL LECTIN,PROTEIN,LINES,ACTIVATION},
  language     = {eng},
  number       = {4},
  pages        = {10},
  title        = {GalNAc/Gal-binding Rhizoctonia solani agglutinin has antiproliferative activity in Drosophila melanogaster S2 cells via MAPK and JAK/STAT signaling},
  url          = {http://dx.doi.org/10.1371/journal.pone.0033680},
  volume       = {7},
  year         = {2012},
}

Chicago
Hamshou, Mohamad, Els Van Damme, Gianni Vandenborre, Bart Ghesquière, Geert Trooskens, Kris Gevaert, and Guy Smagghe. 2012. “GalNAc/Gal-binding Rhizoctonia Solani Agglutinin Has Antiproliferative Activity in Drosophila Melanogaster S2 Cells via MAPK and JAK/STAT Signaling.” Plos One 7 (4).
APA
Hamshou, M., Van Damme, E., Vandenborre, G., Ghesquière, B., Trooskens, G., Gevaert, K., & Smagghe, G. (2012). GalNAc/Gal-binding Rhizoctonia solani agglutinin has antiproliferative activity in Drosophila melanogaster S2 cells via MAPK and JAK/STAT signaling. PLOS ONE, 7(4).
Vancouver
1.
Hamshou M, Van Damme E, Vandenborre G, Ghesquière B, Trooskens G, Gevaert K, et al. GalNAc/Gal-binding Rhizoctonia solani agglutinin has antiproliferative activity in Drosophila melanogaster S2 cells via MAPK and JAK/STAT signaling. PLOS ONE. 2012;7(4).
MLA
Hamshou, Mohamad, Els Van Damme, Gianni Vandenborre, et al. “GalNAc/Gal-binding Rhizoctonia Solani Agglutinin Has Antiproliferative Activity in Drosophila Melanogaster S2 Cells via MAPK and JAK/STAT Signaling.” PLOS ONE 7.4 (2012): n. pag. Print.