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USA , — First in vitro synthesis of the complete lipid-linked N -glycan of C. Jones, M. Structure and synthesis of polyisoprenoids used in N-glycosylation across the three domains of life. Acta , — Burda, P. The dolichol pathway of N -linked glycosylation.

Abu-Qarn, M. Not just for Eukarya anymore: protein glycosylation in Bacteria and Archaea. Chaban, B. Identification of genes involved in the biosynthesis and attachment of Methanococcus voltae N -linked glycans: insight into N -linked glycosylation pathways in Archaea.

Chen, M. Polyisoprenol specificity in the Campylobacter jejuni N-linked glycosylation pathway. Biochemistry 46 , — From peptide to protein: comparative analysis of the substrate specificity of N-linked glycosylation in Campylobacter jejuni. Chemoenzymatic synthesis of glycopeptides with PglB, a bacterial oligosaccharyl transferase from Campylobacter jejuni. Feldman, M.

Engineering N-linked protein glycosylation with diverse O antigen lipopolysaccharide structures in Escherichia coli. Substrate specificity of bacterial oligosaccharyltransferase suggests a common transfer mechanism for the bacterial and eukaryotic systems.

N-Linked Glycosylation Part 1

N -linked protein glycosylation in a bacterial system. Methods Mol. Structural context for protein N -glycosylation in bacteria: The structure of PEB3, an adhesin from Campylobacter jejuni. Protein Sci. Min, T. Specificity of Campylobacter jejuni adhesin PEB3 for phosphates and structural differences among its ligand complexes.

Slynko, V. NMR structure determination of a segmentally labeled glycoprotein using in vitro glycosylation.

Background

Adaptation of Campylobacter jejuni NCTC to high-level colonization of the avian gastrointestinal tract. Karlyshev, A. The Campylobacter jejuni general glycosylation system is important for attachment to human epithelial cells and in the colonization of chicks. Microbiology , — Campylobacter protein glycosylation affects host cell interactions. Hendrixson, D. Identification of Campylobacter jejuni genes involved in commensal colonization of the chick gastrointestinal tract.

Ding, W. Identification and quantification of glycoproteins using ion-pairing normal-phase liquid chromatography and mass spectrometry. Cell Proteomics 8 , — Larsen, J. N-linked protein glycosylation is required for full competence in Campylobacter jejuni Kakuda, T. Cjc encodes a Campylobacter jejuni glycoprotein that influences invasion of human epithelial cells and colonization of the chick gastrointestinal tract. Davis, L. A Campylobacter jejuni znuA orthologue is essential for growth in low-zinc environments and chick colonization.

Flanagan, R. Examination of Campylobacter jejuni putative adhesins leads to the identification of a new protein, designated FlpA, required for chicken colonization. Mass spectrometric characterization of the surface-associated 42 kDa lipoprotein JlpA as a glycosylated antigen in strains of Campylobacter jejuni. Proteome Res. N -glycosylated proteins and distinct lipooligosaccharide glycoforms of Campylobacter jejuni target the human C-type lectin receptor MGL.

Study showing that the C. Hacker, J. Pathogenicity islands of virulent bacteria: structure, function and impact on microbial evolution. Maita, N. Comparative structural biology of Eubacterial and Archaeal oligosaccharyltransferases. Igura, M. Structure-guided identification of a new catalytic motif of oligosaccharyltransferase. Nakagawa, S. Deep-sea vent epsilon-proteobacterial genomes provide insights into emergence of pathogens. Baar, C. Complete genome sequence and analysis of Wolinella succinogenes. Loman, N. Genome sequence of the emerging pathogen Helicobacter canadensis.

Jervis, A. Characterisation of N -linked protein glycosylation in Helicobacter pullorum. Description of another bacterial N -glycosylation pathway resembling the C. Hug, I. Helicobacter pylori lipopolysaccharide is synthesized via a novel pathway with an evolutionary connection to protein N -glycosylation. PLoS Pathog. Fox, J. The non- H. Gut 50 , — Mobley, H. Santos-Silva, T. Crystal structure of the 16 heme cytochrome from Desulfovibrio gigas : a glycosylated protein in a sulphate-reducing bacterium. Gross, J. The Haemophilus influenzae HMW1 adhesin is a glycoprotein with an unusual N -linked carbohydrate modification.

Geme, J.

Protein Glycosylation Labeling Service- Creative BioMart

The HMW1 adhesin of nontypeable Haemophilus influenzae recognizes sialylated glycoprotein receptors on cultured human epithelial cells. Grass, S. The Haemophilus influenzae HMW1 adhesin is glycosylated in a process that requires HMW1C and phosphoglucomutase, an enzyme involved in lipooligosaccharide biosynthesis.

Recent publication describing the unusual N -linked protein glycosylation system of Haemophilus influenzae. Benz, I. Glycosylation with heptose residues mediated by the aah gene product is essential for adherence of the AIDA-I adhesin. Lindenthal, C. Identification of a glycoprotein produced by enterotoxigenic Escherichia coli. Sherlock, O. Glycosylation of the self-recognizing Escherichia coli Ag43 autotransporter protein. Charbonneau, M. Logan, S. Flagellar glycosylation — a new component of the motility repertoire?

Review on bacterial flagellar glycosylation. Ng, S. Archaeal flagella, bacterial flagella and type IV pili: a comparison of genes and posttranslational modifications. Thibault, P. Identification of the carbohydrate moieties and glycosylation motifs in Campylobacter jejuni flagellin. Goon, S. Pseudaminic acid, the major modification on Campylobacter flagellin , is synthesized via the Cj gene.

Guerry, P. Campylobacter flagella: not just for motility. Trends Microbiol. Review summarizing the biological functions of O -linked flagella glycosylation in Campylobacter spp. Campylobacter sugars sticking out. Champion, O. Comparative phylogenomics of the food-borne pathogen Campylobacter jejuni reveals genetic markers predictive of infection source.

Howard, S.

Gene Ontology Term: protein glycosylation

Campylobacter jejuni glycosylation island important in cell charge, legionaminic acid biosynthesis, and colonization of chickens. McNally, D. Functional characterization of the flagellar glycosylation locus in Campylobacter jejuni using a focused metabolomics approach. Schirm, M.

Identification of unusual bacterial glycosylation by tandem mass spectrometry analyses of intact proteins. Changes in flagellin glycosylation affect Campylobacter autoagglutination and virulence. Ewing, C. Functional characterization of flagellin glycosylation in Campylobacter jejuni Glycobiology 19 , — Josenhans, C. FEMS Microbiol. Structural, genetic and functional characterization of the flagellin glycosylation process in Helicobacter pylori. Glycobiology 16 , 8C—14C Twine, S. Flagellar glycosylation in Clostridium botulinum.

FEBS J. Motility and flagellar glycosylation in Clostridium difficile. Allison, J. Electrophoretic separation and molecular weight characterization of Pseudomonas aeruginosa H-antigen flagellins. Lanyi, B. Serological properties of Pseudomonas aeruginosa. Type-specific thermolabile flagellar antigens. Learn more. Protein glycosylation is ubiquitous in biological systems and plays essential roles in many cellular events. However, it is extraordinarily challenging because of the low abundance of many glycoproteins and the heterogeneity of glycan structures. We next discuss the systematic and quantitative analysis of glycoprotein dynamics.

Reversible protein glycosylation is dynamic, and systematic study of glycoprotein dynamics helps us gain insight into glycoprotein functions. Intact glycopeptide analysis is also included in this section. Because of the importance of glycoproteins in complex biological systems, the field of glycoproteomics will continue to grow in the next decade. Volume 38 , Issue The full text of this article hosted at iucr. If you do not receive an email within 10 minutes, your email address may not be registered, and you may need to create a new Wiley Online Library account.

If the address matches an existing account you will receive an email with instructions to retrieve your username. Thus, potentially determining function of AC8 in cells where it is expressed. This would imply a differential localization and functional role for AC8-B. Glycosylation of AC6 is required for response to several stimulators of AC activity since mutagenesis or glycosylation inhibitors affect AC6 response to forskolin and G-proteins [ 38 ].

The other member of the calcium-inhibited ACs, AC5, has two putative glycosylation sites but it is still unclear as to whether these sites are glycosylated [ 36 ]. The other member of the adenylate cyclase family of enzymes is adenylate cyclase 9 AC9.


  • Eukaryotic protein glycosylation: a primer for histochemists and cell biologists?
  • Ship of Fools?
  • AmiGO 2: Term Details for "protein glycosylation" (GO).

This particular adenylate cyclase is the most divergent in terms of sequence from the other known ACs. AC9 activity is regulated by G-proteins and by protein kinase C. AC9 is glycosylated on two sites; removal of the N-linked glycosylation on these sites by site directed mutagenesis did not affect the stimulation of AC9 by forskolin [ 39 ].

Taken together, these data reveal an integral role for glycosylation in determining and modulating adenylate cyclase localization, protein-protein interactions and function. The insulin receptor is a hetero-tetrameric receptor tyrosine kinase that is well known for its regulation of glucose metabolism. The insulin receptor contains numerous glycosylation sites that include both O- and N-linked glycosylation. The glycosylation of the insulin receptor is metabolically regulated since glucose deprivation has been shown to preferentially affect O-linked but not N-linked glycosylation of the receptor.

Indeed, mutational analysis of the potential O-glycosylation sites on the insulin receptor has revealed significant effects on functioning of the receptor. This may be due to the fact that these sites tend to be near phosphorylation sites on the receptor important to regulation of the receptor activity [ 41 ].

Removal of glycosylation on the receptor does not affect receptor binding but partial loss of glycosylation leads to a constitutively active kinase activity of the receptor. These data demonstrate that glycosylation is a key regulator of insulin receptor function. Taken together with the observation that the glycemic state of the cell can modulate the pattern of glycosylation of the receptor [ 40 , 43 ], these data suggest that insulin receptor activity is dynamically regulated within insulin target cells and is sensitive to the metabolic state of the cell. In addition to the insulin receptor, insulin signaling molecules have been found to be regulated by glycosylation.

Furthermore, it is thought that shunting of glucose metabolism through the hexosamine biosynthetic pathway leads to a general increase in O-linked glycosylation of nuclear and cytoplasmic proteins through increased substrate for O-linked N-acetylglucosamine transferase [ 41 ]. The end result of this process is loss of cellular insulin sensitivity [ 41 ].

It is now well documented that most GPCRs have the capability of signaling via multiple pathways in a given cell type. For many years, this hypothesis was poorly understood and was thought to be an artifact of recombinant cell systems. With the recent development of allosteric agonists, antagonists and modulators to GPCRs, more light has been shed on this concept; e. This phenomenon has most recently been termed, biased signaling. Simply put, the concept of biased signaling describes the ability of ligands to direct specific and distinct biological responses via activation of select signaling pathways in a ligand-specific manner [ 4 ].

There are many receptors that are known to associate with multiple naturally occurring ligands. Since varying glycosylation of gonadotropin isoforms is known to alter their physicochemical properties, one can consider gonadotropin isoforms as different ligands with potentially subtle, but unique association with their cognate receptors [ 4 , 24 ]. In addition, interaction of these diverse ligands with the receptor would result in multiple ligand-receptor conformations, which in turn lead to the observed activation of differing biological signaling pathways for LH, hCG and FSH [ 13 , 45 , 46 ].

Thus, it has been suggested that gonadotropin isforms are naturally occurring biased agonists for their receptors [ 4 , 24 ]. The molecular basis for biased agonism lies in the stabilization of conformation s of the receptor which increases the affinity of the biased agonist-receptor complex for a distinct and specific signaling pathway over another [ 44 ]. Since GPCRs primarily utilize G proteins as signal transducers, biased agonism would imply ligand-dependent preference of the ligand-receptor complex for a specific G-protein over another. Glycosylated variants of gonadotropins are biased agonists at their receptors.

Gonadotropins are secreted into the blood as isoforms that vary in the degree of complexity of glycosylation. Variations in glycosylation has been shown to be important to plasma half-life and receptor binding. It is now appreciated that these isoforms also impact the biological activity of the gonadotropins [4].

In the case of FSH depicted , glycosylated variants stabilize different conformations of the receptor-ligand complex. This leads to different affinities of the receptor-ligand complex for association with G proteins. Highly complex, terminally sialylated FSH induces activation of Gs signaling pathways. Less complex glycosylation associated with terminal mannose leads to activation of both Gs and Gi signaling pathways.

Deglycosylated FSH activates the Gi signaling pathway. Since the FSHR is also know to affect other signaling pathways, such as Gq, these isoforms may also differentially activate Gq signaling as well. For many years, FSH has been used as a model to understand the role of glycosylation in determining glycoprotein hormone function. Several years ago, we noted that differently glycosylated variants of hFSH could induce activation of both the Gs and Gi signaling pathways [ 24 , 47 ].

The phenomenon appeared as a bell-shaped concentration-response curve in in vitro assay systems for less glycosylated insect cell expressed hFSH BV-hFSH. Pertussis toxin was found to block the down-turn in the dose-response relationship, indicating that thedescending phase of the curve for the BV-hFSH was due to activation of Gi at higher concentrations of the hormone.

These pharmacological relationships had been described previously for other receptors such as the catacholamines and adenosine receptors [ 48 , 49 ]. In the case of the insect cell expressed hFSH BV-hFSH , glycosylation was terminated at short branched mannose residues, and the protein displayed a more basic migration pattern in chromatofocusing Arey, unpublished data. Subsequent experiments using an ADP-ribosylation assay, along with immunoprecipitation and Western blotting of specific G-proteins, revealed that these pharmacological responses were definitively associated with activation of specific G-proteins [ 50 ].

1. Introduction

Taken together with in vivo effects of the different FSH preparations [ 4 ], these data demonstrate that the activities observed in signaling are directly translated into organ growth responses and illustrate the ability of the biased ligand e. Interestingly, similar glycosylation-dependent signal biasing has been noted for other secreted glycoproteins e.

In the case of BMP6, detailed mutagenesis around key asparagine residues has revealed the importance of glycosylation in interactions with its receptor [ 52 ]. In the case of IL22, a single fucose residue on Asn54 was shown to be required for full efficacy of the cytokine at its receptor. It is worth mentioning that the binding kinetics of the receptor were altered bymore complex glycosylation at this site [ 51 ]. Similar but more dramatic effects of glycosylation on binding kinetics have also been noted for erythropoeitin [ 56 ]. These examples lay the foundation for the concept that a variety of related natural ligands talk to the receptor by inducing specific receptor conformations and that glycosylation plays a role in aiding in this stabilization, thus transducing specific signals that are unique to a given physiological state.

Similar activities were ultimately discovered for other GPCRs [ 57 ]. Therefore, from a mechanistic viewpoint, there is strong support for the notion that alteration of the glycosylation pattern on glycoprotein hormones leads to biased ligands that direct activation of one signaling pathway over another. Therefore, different glycosylated variants may interact with the receptor in subtle, but unique ways to result in different signaling and biological responses. Licensee IntechOpen. This chapter is distributed under the terms of the Creative Commons Attribution 3. Help us write another book on this subject and reach those readers.

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