Global Identification of Prokaryotic Glycoproteins Based on an Escherichia coli Proteome Microarray

Zong xiu Wang, Rui ping Deng, He Wei Jiang, Shu Juan Guo, Huang ying Le, Xiao dong Zhao, Chien Sheng Chen, Ji bin Zhang, Sheng ce Tao

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)


Glycosylation is one of the most abundant protein posttranslational modifications. Protein glycosylation plays important roles not only in eukaryotes but also in prokaryotes. To further understand the roles of protein glycosylation in prokaryotes, we developed a lectin binding assay to screen glycoproteins on an Escherichia coli proteome microarray containing 4,256 affinity-purified E.coli proteins. Twenty-three E.coli proteins that bound Wheat-Germ Agglutinin (WGA) were identified. PANTHER protein classification analysis showed that these glycoprotein candidates were highly enriched in metabolic process and catalytic activity classes. One sub-network centered on deoxyribonuclease I (sbcB) was identified. Bioinformatics analysis suggests that prokaryotic protein glycosylation may play roles in nucleotide and nucleic acid metabolism. Fifteen of the 23 glycoprotein candidates were validated by lectin (WGA) staining, thereby increasing the number of validated E. coli glycoproteins from 3 to 18. By cataloguing glycoproteins in E.coli, our study greatly extends our understanding of protein glycosylation in prokaryotes.

Original languageEnglish
Article numbere49080
JournalPloS one
Issue number11
Publication statusPublished - 2012 Nov 7

All Science Journal Classification (ASJC) codes

  • General


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