Glycosylation signatures in Drosophila : fishing with lectins
- Author
- Gianni Vandenborre (UGent) , Els Van Damme (UGent) , Bart Ghesquière (UGent) , Gerben Menschaert (UGent) , Mohamad Hamshou (UGent) , Rameshwaram Nagender Rao, Kris Gevaert (UGent) and Guy Smagghe (UGent)
- Organization
- Abstract
- Glycosylation is a co- and/or post-translational protein modification that generates enormous structural diversity among glycoproteins. In this study, immobilized lectins were used to capture glycoproteins with different glycan profiles from Drosophila melanogaster extracts. On the basis of previous results from glycan array analyses, the snowdrop (Galanthus nivalis) agglutinin (GNA), the tobacco (Nicotiana tabacum) lectin (Nictaba) and the Rhizoctoni solani agglutinin (RSA) were used to select for a broad range of N- and O-glycan structures. After different lectin affinity chromatographies, the glycoproteome of Drosophila was analyzed using LC-MS/MS and glycoprotein abundances were calculated by different label-free methods. Bioinformatics tools were used to annotate the identified glycoproteins and the glycoproteins were classified according to their molecular function or their involvement in a biological process. Subsequent enrichment analysis (using the DAVID database) was employed to find biological processes or molecular functions in Drosophila in which a particular glycan signature is overrepresented. The results presented here clearly demonstrate that next to the presence of high-mannose and paucimannose N-glycans, Drosophila is capable of synthesizing glycoproteins carrying extended hybrid and complex N-linked glycans. Furthermore, it was demonstrated that a specific glycosylation signature can be associated with a functionally related group of glycoproteins in Drosophila, both in terms of biological process and molecular function.
- Keywords
- MOUSE, PROTEIN, MELANOGASTER, N-GLYCANS, TANDEM MASS-SPECTROMETRY, lectins, Drosophila melanogaster glycan profiles, glycoproteins, GLYCOPROTEOMICS, SPECIFICITY, COMPLEXITY, INSIGHTS, SNOWDROP
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Citation
Please use this url to cite or link to this publication: http://hdl.handle.net/1854/LU-935578
- MLA
- Vandenborre, Gianni, et al. “Glycosylation Signatures in Drosophila : Fishing with Lectins.” JOURNAL OF PROTEOME RESEARCH, vol. 9, no. 6, 2010, pp. 3235–42, doi:10.1021/pr1001753.
- APA
- Vandenborre, G., Van Damme, E., Ghesquière, B., Menschaert, G., Hamshou, M., Rao, R. N., … Smagghe, G. (2010). Glycosylation signatures in Drosophila : fishing with lectins. JOURNAL OF PROTEOME RESEARCH, 9(6), 3235–3242. https://doi.org/10.1021/pr1001753
- Chicago author-date
- Vandenborre, Gianni, Els Van Damme, Bart Ghesquière, Gerben Menschaert, Mohamad Hamshou, Rameshwaram Nagender Rao, Kris Gevaert, and Guy Smagghe. 2010. “Glycosylation Signatures in Drosophila : Fishing with Lectins.” JOURNAL OF PROTEOME RESEARCH 9 (6): 3235–42. https://doi.org/10.1021/pr1001753.
- Chicago author-date (all authors)
- Vandenborre, Gianni, Els Van Damme, Bart Ghesquière, Gerben Menschaert, Mohamad Hamshou, Rameshwaram Nagender Rao, Kris Gevaert, and Guy Smagghe. 2010. “Glycosylation Signatures in Drosophila : Fishing with Lectins.” JOURNAL OF PROTEOME RESEARCH 9 (6): 3235–3242. doi:10.1021/pr1001753.
- Vancouver
- 1.Vandenborre G, Van Damme E, Ghesquière B, Menschaert G, Hamshou M, Rao RN, et al. Glycosylation signatures in Drosophila : fishing with lectins. JOURNAL OF PROTEOME RESEARCH. 2010;9(6):3235–42.
- IEEE
- [1]G. Vandenborre et al., “Glycosylation signatures in Drosophila : fishing with lectins,” JOURNAL OF PROTEOME RESEARCH, vol. 9, no. 6, pp. 3235–3242, 2010.
@article{935578,
abstract = {{Glycosylation is a co- and/or post-translational protein modification that generates enormous structural diversity among glycoproteins. In this study, immobilized lectins were used to capture glycoproteins with different glycan profiles from Drosophila melanogaster extracts. On the basis of previous results from glycan array analyses, the snowdrop (Galanthus nivalis) agglutinin (GNA), the tobacco (Nicotiana tabacum) lectin (Nictaba) and the Rhizoctoni solani agglutinin (RSA) were used to select for a broad range of N- and O-glycan structures. After different lectin affinity chromatographies, the glycoproteome of Drosophila was analyzed using LC-MS/MS and glycoprotein abundances were calculated by different label-free methods. Bioinformatics tools were used to annotate the identified glycoproteins and the glycoproteins were classified according to their molecular function or their involvement in a biological process. Subsequent enrichment analysis (using the DAVID database) was employed to find biological processes or molecular functions in Drosophila in which a particular glycan signature is overrepresented. The results presented here clearly demonstrate that next to the presence of high-mannose and paucimannose N-glycans, Drosophila is capable of synthesizing glycoproteins carrying extended hybrid and complex N-linked glycans. Furthermore, it was demonstrated that a specific glycosylation signature can be associated with a functionally related group of glycoproteins in Drosophila, both in terms of biological process and molecular function.}},
author = {{Vandenborre, Gianni and Van Damme, Els and Ghesquière, Bart and Menschaert, Gerben and Hamshou, Mohamad and Rao, Rameshwaram Nagender and Gevaert, Kris and Smagghe, Guy}},
issn = {{1535-3893}},
journal = {{JOURNAL OF PROTEOME RESEARCH}},
keywords = {{MOUSE,PROTEIN,MELANOGASTER,N-GLYCANS,TANDEM MASS-SPECTROMETRY,lectins,Drosophila melanogaster glycan profiles,glycoproteins,GLYCOPROTEOMICS,SPECIFICITY,COMPLEXITY,INSIGHTS,SNOWDROP}},
language = {{eng}},
number = {{6}},
pages = {{3235--3242}},
title = {{Glycosylation signatures in Drosophila : fishing with lectins}},
url = {{http://doi.org/10.1021/pr1001753}},
volume = {{9}},
year = {{2010}},
}
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