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Journal ArticleDOI

Glycoproteins in prokaryotes

S. Moens, +1 more
- 01 Sep 1997 - 
- Vol. 168, Iss: 3, pp 169-175
TLDR
From the fragmented data available for the prokaryotic glycoproteins, similarities with the eukaryotic system can be noticed.
Abstract
Rather recently it has become clear that prokaryotes (Archaea and Bacteria) are able to glycosylate proteins. A literature survey revealed the different types of glycoproteins. They include mainly surface layer (S-layer) proteins, flagellins, and polysaccharide-degrading enzymes. Only in a few cases is structural information available. Many different structures have been observed that display much more variation than that observed in eukaryotes. A few studies have given evidence for the function of the prokaryotic glycoprotein glycans. Also from the biosynthetic point of view, information is rather scarce. Due to their different cell structure, prokaryotes have to use mechanisms different from those found in eukaryotes to glycosylate proteins. However, from the fragmented data available for the prokaryotic glycoproteins, similarities with the eukaryotic system can be noticed.

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Citations
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Roles of N-Linked Glycans in the Endoplasmic Reticulum

TL;DR: From a process involved in cell wall synthesis in archaea and some bacteria, N-linked glycosylation has evolved into the most common covalent protein modification in eukaryotic cells.
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Type V Protein Secretion Pathway: the Autotransporter Story

TL;DR: A review of the autotransporter secretion process in the context of the more general field of bacterial protein translocation and exoprotein function considers the type V secretion pathway.
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Protein glycosylation in bacteria: sweeter than ever.

TL;DR: It is now established that bacteria possess both N-linked and O-linked glycosylation pathways that display many commonalities with their eukaryotic and archaeal counterparts as well as some unexpected variations.
Journal ArticleDOI

Structure of the N-Linked Glycan Present on Multiple Glycoproteins in the Gram-negative Bacterium, Campylobacter jejuni

TL;DR: Comparison of thepgl locus with that of Neisseria meningitidissuggested that most of the homologous genes are probably involved in the biosynthesis of bacillosamine, and at least 22 glycoproteins were identified.
Patent

Methods for producing modified glycoproteins

TL;DR: In this article, a combination of engineering and/or selection of strains which do not express certain enzymes which create the undesirable complex structures characteristic of the fungal glycoproteins, which express exogenous enzymes selected either to have optimal activity under the conditions present in the fungi where activity is desired, or which are targeted to an organelle where optimal activity is achieved.
References
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Journal ArticleDOI

Glycoprotein biosynthesis in yeast

TL;DR: Yeast mutants are useful to identify biosynthetic intermediates, to establish whether a given enzyme is essential for viability, and to determine how cellular functions are affected when glycosylation is perturbed.
Journal ArticleDOI

Phenotypic characterization of the archaebacterial genus Sulfolobus: comparison of five wild-type strains.

TL;DR: Five laboratory strains, including type strains of the described species Sulfolobus acidocaldarius and S. solfataricus, were compared with respect to a variety of growth and biochemical parameters, including component profile of the surface-layer cell wall, inhibitors of growth, growth rate as a function of temperature and pH, and compounds used as sole sources of carbon or nitrogen.
Journal ArticleDOI

Meningococcal pilin: a glycoprotein substituted with digalactosyl 2,4-diacetamido-2,4,6-trideoxyhexose.

TL;DR: These studies have confirmed the previous observations that meningococcal pili are glycosylated and provided the first structural evidence for the presence of covalently linked carbohydrate on pili, and revealed a completely novel protein/saccharide linkage.
Journal ArticleDOI

Structure and biosynthesis of prokaryotic glycoproteins.

TL;DR: The overall structure of the cell surface glycoprotein of halobacteria is thus reminiscent of animal proteoglycans and a functional role of the glycosaminoglycan chain in maintaining the rod shape of Halob bacteria is discussed.
Journal ArticleDOI

Pilus‐facilitated adherence of Neisseria meningitidis to human epithelial and endothelial cells: modulation of adherence phenotype occurs concurrently with changes in primary amino acid sequence and the glycosylation status of pilin

TL;DR: It is proposed that functional variations in N. meningitidis pili may be modulated in large part by primary amino acid sequence changes that ablate or create N‐linked glycosylation sites on the pilin subunit.
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