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Taxonomic group: bacteria / Proteobacteria (Phylum: Proteobacteria)
Associated disease: infection due to Campylobacter jejuni [ICD11: XN4Q5

]

NCBI PubMed ID: 18816436
Publication DOI: 10.1002/smll.200701215
Journal NLM ID: 101235338
Publisher: Weinheim: Wiley-VCH
Correspondence: christina.schaeffer

boku.ac.at
Institutions: University of Natural Resources and Applied Life Sciences, Center for NanoBiotechnology, Gregor-Mendel-Strasse 33, A-1180 Wien, Austria

Crucial biological phenomena are mediated through carbohydrates that are displayed in a defined manner and interact with molecular scale precision. We lay the groundwork for the integration of recombinant carbohydrates into a 'biomolecular construction kit' for the design of new biomaterials, by utilizing the self-assembly system of the crystalline cell surface (S)-layer protein SgsE of Geobacillus stearothermophilus NRS 2004/3a. SgsE is a naturally O-glycosylated protein, with intrinsic properties that allow it to function as a nanopatterned matrix for the periodic display of glycans. By using a combined carbohydrate/protein engineering approach, two types of S-layer neoglycoproteins are produced in Escherichia coli. Based on the identification of a suitable periplasmic targeting system for the SgsE self-assembly protein as a cellular prerequisite for protein glycosylation, and on engineering of one of the natural protein O-glycosylation sites into a target for N-glycosylation, the heptasaccharide from the AcrA protein of Campylobacter jejuni and the O7 polysaccharide of E. coli are co- or post-translationally transferred to the S-layer protein by the action of the oligosaccharyltransferase PglB. The degree of glycosylation of the S-layer neoglycoproteins after purification from the periplasmic fraction reaches completeness. Electron microscopy reveals that recombinant glycosylation is fully compatible with the S-layer protein self-assembly system. Tailor-made ('functional') nanopatterned, self-assembling neoglycoproteins may open up new strategies for influencing and controlling complex biological systems with potential applications in the areas of biomimetics, drug targeting, vaccine design, or diagnostics.

Self-assembly, biomimetics, composites, protein engineering, S-layers

Structure type: oligomer
Location inside paper: p.1729
Trivial name: heptasaccharide, free OS
Compound class: N-glycan
Contained glycoepitopes: IEDB_130648,IEDB_137473,IEDB_1391961,IEDB_141584,IEDB_142488,IEDB_146664,IEDB_885822,IEDB_983931,SB_192

Methods: SDS-PAGE, MALDI-TOF MS, serological methods, genetic methods, electron microscopy
Biological activity: serological data
Enzymes that release or process the structure: Pgl
Biosynthesis and genetic data: genetic data
3D data: 3D data, modeling of nanopatterned neoglycoproteins

Related record ID(s): 23640
NCBI Taxonomy refs (TaxIDs): 197
Reference(s) to other database(s): GTC:G58528CE, GlycomeDB:37258
Show glycosyltransferases

There is only one chemically distinct structure:

CC(=O)N[C@H]1[C@@H](O)O[C@H](C)[C@@H](NC(C)=O)[C@@H]1O[C@H]1O[C@H](CO)[C@H](O[C@H]2O[C@H](CO)[C@H](O[C@H]3O[C@H](CO)[C@H](O[C@H]4O[C@H](CO)[C@H](O[C@H]5O[C@H](CO)[C@H](O)[C@H](O)[C@H]5NC(C)=O)[C@H](O)[C@H]4NC(C)=O)[C@H](O[C@@H]4O[C@H](CO)[C@@H](O)[C@H](O)[C@H]4O)[C@H]3NC(C)=O)[C@H](O)[C@H]2NC(C)=O)[C@H](O)[C@H]1NC(C)=O

SVG MW SMILES 3D mol Ionize