Skip to main content

Prediction of Cell Specific O-GalNAc Glycosylation in Human

  • Conference paper
  • First Online:
Data Science (ICPCSEE 2017)

Part of the book series: Communications in Computer and Information Science ((CCIS,volume 728))

  • 1674 Accesses

Abstract

Glycosylation is one of the most extensive post-translation modifications of proteins. Although lots of computational models have been developed to predict the glycosylation sites, none of them considered the tissue and cell specificity of glycosylation. Here, we built a two-step computational method GlycoCell to predict the cell-specific O-GalNAc glycosylation, the most complex type of O-glycosylation reported so far, in 12 human cell types. The first step predicted whether a site had the potential to be O-glycosylated. The model achieved an accuracy of 0.83. The second step predicted whether a potential glycosite would be O-glycosylated in the given cell type. For 12 cell types, a model was built for each cell type. The accuracies for these models ranged from 0.78 to 0.87. To facilitate the usage of GlycoCell for the public, a web server was built which is available at http://www.biomedcloud.com.cn/GlyoCell/main.htm. It could be useful for investigating the cell-specific O-glycosylation in human.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 39.99
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 54.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

References

  1. Wright, A., Morrison, S.L.: Effect of glycosylation on antibody function: implications for genetic engineering. Trends Biotechnol. 15(1), 26–32 (1997)

    Article  Google Scholar 

  2. Arnold, J.N., et al.: The impact of glycosylation on the biological function and structure of human immunoglobulins. Annu. Rev. Immunol. 25, 21–50 (2007)

    Article  Google Scholar 

  3. Moremen, K.W., Tiemeyer, M., Nairn, A.V.: Vertebrate protein glycosylation: diversity, synthesis and function. Nat. Rev. Mol. Cell Biol. 13(7), 448–462 (2012)

    Article  Google Scholar 

  4. Chauhan, J.S., Rao, A., Raghava, G.P.S.: In silico platform for prediction of N-, O-and C-glycosites in eukaryotic protein sequences. PloS one 8(6), e67008 (2013)

    Article  Google Scholar 

  5. Li, F., et al.: GlycoMine: a machine learning-based approach for predicting N-, C-and O-linked glycosylation in the human proteome. Bioinformatics 31, 1411–1419 (2015). btu852

    Article  Google Scholar 

  6. Bennett, E.P., et al.: Control of mucin-type O-glycosylation: a classification of the polypeptide GalNAc-transferase gene family. Glycobiology 22(6), 736–756 (2012)

    Article  Google Scholar 

  7. Steentoft, C., et al.: Precision mapping of the human O-GalNAc glycoproteome through SimpleCell technology. The EMBO J. 32(10), 1478–1488 (2013)

    Article  Google Scholar 

  8. Müller, S., Hanisch, F.-G.: Recombinant MUC1 probe authentically reflects cell-specific o-glycosylation profiles of endogenous breast cancer mucin. High density and prevalent core 2-based glycosylation. J. Biol. Chem. 277(29), 26103–26112 (2002)

    Article  Google Scholar 

  9. Romanova, J., et al.: Distinct host range of influenza H3N2 virus isolates in Vero and MDCK cells is determined by cell specific glycosylation pattern. Virology 307(1), 90–97 (2003)

    Article  Google Scholar 

  10. Christensen, B., et al.: Cell type-specific post-translational modifications of mouse osteopontin are associated with different adhesive properties. J. Biol. Chem. 282(27), 19463–19472 (2007)

    Article  Google Scholar 

  11. Hansen, J.E., et al.: NetOglyc: prediction of mucin type O-glycosylation sites based on sequence context and surface accessibility. Glycoconjugate J. 15(2), 115–130 (1998)

    Article  Google Scholar 

  12. UniProt. (2016). http://www.uniprot.org/

  13. Asgari, E., Mofrad, M.R.K.: Continuous distributed representation of biological sequences for deep proteomics and genomics. PLoS ONE 10(11), e0141287 (2015)

    Article  Google Scholar 

  14. Hu, Q.: The Research on Protein Sequence Feature Extraction and Its Application on Protein Subcellular Location. Hunan University, Changsha (2013)

    Google Scholar 

  15. O’Connell, B.C., Hagen, F.K., Tabak, L.A.: The influence of flanking sequence on the O-glycosylation of threonine in vitro. J. Biol. Chem. 267(35), 25010–25018 (1992)

    Google Scholar 

Download references

Acknowledgements

This study was supported by the National Natural Science Foundation (31500126 and 31371338), the National Key Plan for Scientific Research and Development of China (2016YFD0500300 and 2016YFC1200200) and the International Scientific and Technological Cooperation project (2014DFB30010).

There are no conflicts of interest.

Author information

Authors and Affiliations

Authors

Corresponding authors

Correspondence to Taijiao Jiang or Yousong Peng .

Editor information

Editors and Affiliations

1 Electronic supplementary material

Below is the link to the electronic supplementary material.

Supplementary material 1 (docx 117 KB)

Rights and permissions

Reprints and permissions

Copyright information

© 2017 Springer Nature Singapore Pte Ltd.

About this paper

Cite this paper

Zou, Y., Li, K., Jiang, T., Peng, Y. (2017). Prediction of Cell Specific O-GalNAc Glycosylation in Human. In: Zou, B., Han, Q., Sun, G., Jing, W., Peng, X., Lu, Z. (eds) Data Science. ICPCSEE 2017. Communications in Computer and Information Science, vol 728. Springer, Singapore. https://doi.org/10.1007/978-981-10-6388-6_23

Download citation

  • DOI: https://doi.org/10.1007/978-981-10-6388-6_23

  • Published:

  • Publisher Name: Springer, Singapore

  • Print ISBN: 978-981-10-6387-9

  • Online ISBN: 978-981-10-6388-6

  • eBook Packages: Computer ScienceComputer Science (R0)

Publish with us

Policies and ethics