CSDB: Search results

Taxonomic group: bacteria / Proteobacteria (Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11: XN6P4

]

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: suggested polymer biological repeating unit
Location inside paper: p.1729
The structure in this paper was incorrect:

Original structure from CSDB record 23640

← originally published structure

Show legend

Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_130701,IEDB_136044,IEDB_136105,IEDB_137340,IEDB_137472,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_144983,IEDB_150899,IEDB_151531,IEDB_152206,IEDB_190606,IEDB_225177,IEDB_885823,IEDB_983930,SB_137,SB_165,SB_166,SB_187,SB_195,SB_29,SB_44,SB_67,SB_7,SB_72,SB_88

Methods: SDS-PAGE, MALDI-TOF MS, serological methods, genetic methods, electron microscopy
Biological activity: serological data
Biosynthesis and genetic data: genetic data
Comments, role: the structure in paper is incorrect, as well as in the cited reference; both were revised basing on later studies
3D data: 3D data, modeling of nanopatterned neoglycoproteins

Related record ID(s): 2162, 10463, 11786, 20641, 23054, 23944, 29648, 30268, 108701, 114155, 116994
NCBI Taxonomy refs (TaxIDs): 2162916
Reference(s) to other database(s): GTC:G32754QY, GlycomeDB:37262
Show glycosyltransferases

There is only one chemically distinct structure:

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

SVG MW SMILES 3D mol Ionize