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Diversity in protein glycosylation among insect species

Gianni Vandenborre UGent, Guy Smagghe UGent, Bart Ghesquière UGent, Gerben Menschaert UGent, Nagender Rao UGent, Kris Gevaert UGent and Els Van Damme UGent (2011) PLOS ONE. 6(2).
abstract
Background: A very common protein modification in multicellular organisms is protein glycosylation or the addition of carbohydrate structures to the peptide backbone. Although the Class of the Insecta is the largest animal taxon on Earth, almost all information concerning glycosylation in insects is derived from studies with only one species, namely the fruit fly Drosophila melanogaster. Methodology/Principal Findings: In this report, the differences in glycoproteomes between insects belonging to several economically important insect orders were studied. Using GNA (Galanthus nivalis agglutinin) affinity chromatography, different sets of glycoproteins with mannosyl-containing glycan structures were purified from the flour beetle (Tribolium castaneum), the silkworm (Bombyx mori), the honeybee (Apis mellifera), the fruit fly (D. melanogaster) and the pea aphid (Acyrthosiphon pisum). To identify and characterize the purified glycoproteins, LC-MS/MS analysis was performed. For all insect species, it was demonstrated that glycoproteins were related to a broad range of biological processes and molecular functions. Moreover, the majority of glycoproteins retained on the GNA column were unique to one particular insect species and only a few glycoproteins were present in the five different glycoprotein sets. Furthermore, these data support the hypothesis that insect glycoproteins can be decorated with mannosylated O-glycans. Conclusions/Significance: The results presented here demonstrate that oligomannose N-glycosylation events are highly specific depending on the insect species. In addition, we also demonstrated that protein O-mannosylation in insect species may occur more frequently than currently believed.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
PEA APHID, GLYCOSYLTRANSFERASE, DROSOPHILA-MELANOGASTER, SPODOPTERA-LITTORALIS, O-MANNOSYLTRANSFERASE ACTIVITY, NILAPARVATA-LUGENS, SNOWDROP LECTIN, FERRITIN ACTS, BOMBYX-MORI, CELL-ADHESION
journal title
PLOS ONE
PLoS One
volume
6
issue
2
article_number
e16682
pages
9 pages
Web of Science type
Article
Web of Science id
000287657500014
JCR category
BIOLOGY
JCR impact factor
4.092 (2011)
JCR rank
12/84 (2011)
JCR quartile
1 (2011)
ISSN
1932-6203
DOI
10.1371/journal.pone.0016682
language
English
UGent publication?
yes
classification
A1
copyright statement
I have retained and own the full copyright for this publication
id
1197666
handle
http://hdl.handle.net/1854/LU-1197666
date created
2011-03-28 10:30:30
date last changed
2013-01-30 09:41:19
@article{1197666,
  abstract     = {Background: A very common protein modification in multicellular organisms is protein glycosylation or the addition of carbohydrate structures to the peptide backbone. Although the Class of the Insecta is the largest animal taxon on Earth, almost all information concerning glycosylation in insects is derived from studies with only one species, namely the fruit fly Drosophila melanogaster.
Methodology/Principal Findings: In this report, the differences in glycoproteomes between insects belonging to several economically important insect orders were studied. Using GNA (Galanthus nivalis agglutinin) affinity chromatography, different sets of glycoproteins with mannosyl-containing glycan structures were purified from the flour beetle (Tribolium castaneum), the silkworm (Bombyx mori), the honeybee (Apis mellifera), the fruit fly (D. melanogaster) and the pea aphid (Acyrthosiphon pisum). To identify and characterize the purified glycoproteins, LC-MS/MS analysis was performed. For all insect species, it was demonstrated that glycoproteins were related to a broad range of biological processes and molecular functions. Moreover, the majority of glycoproteins retained on the GNA column were unique to one particular insect species and only a few glycoproteins were present in the five different glycoprotein sets. Furthermore, these data support the hypothesis that insect glycoproteins can be decorated with mannosylated O-glycans.
Conclusions/Significance: The results presented here demonstrate that oligomannose N-glycosylation events are highly specific depending on the insect species. In addition, we also demonstrated that protein O-mannosylation in insect species may occur more frequently than currently believed.},
  articleno    = {e16682},
  author       = {Vandenborre, Gianni and Smagghe, Guy and Ghesqui{\`e}re, Bart and Menschaert, Gerben and Rao, Nagender and Gevaert, Kris and Van Damme, Els},
  issn         = {1932-6203},
  journal      = {PLOS ONE},
  keyword      = {PEA APHID,GLYCOSYLTRANSFERASE,DROSOPHILA-MELANOGASTER,SPODOPTERA-LITTORALIS,O-MANNOSYLTRANSFERASE ACTIVITY,NILAPARVATA-LUGENS,SNOWDROP LECTIN,FERRITIN ACTS,BOMBYX-MORI,CELL-ADHESION},
  language     = {eng},
  number       = {2},
  pages        = {9},
  title        = {Diversity in protein glycosylation among insect species},
  url          = {http://dx.doi.org/10.1371/journal.pone.0016682},
  volume       = {6},
  year         = {2011},
}

Chicago
Vandenborre, Gianni, Guy Smagghe, Bart Ghesquière, Gerben Menschaert, Nagender Rao, Kris Gevaert, and Els Van Damme. 2011. “Diversity in Protein Glycosylation Among Insect Species.” Plos One 6 (2).
APA
Vandenborre, G., Smagghe, G., Ghesquière, B., Menschaert, G., Rao, N., Gevaert, K., & Van Damme, E. (2011). Diversity in protein glycosylation among insect species. PLOS ONE, 6(2).
Vancouver
1.
Vandenborre G, Smagghe G, Ghesquière B, Menschaert G, Rao N, Gevaert K, et al. Diversity in protein glycosylation among insect species. PLOS ONE. 2011;6(2).
MLA
Vandenborre, Gianni, Guy Smagghe, Bart Ghesquière, et al. “Diversity in Protein Glycosylation Among Insect Species.” PLOS ONE 6.2 (2011): n. pag. Print.