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Article: The Tip of

Duncombe, Lucy / Howells, Laurence / Haughey, Anna / Taylor, Andrew V / Kaveh, Daryan / Erdenliğ Gϋrbilek, Sevil / Dell, Anne / Hitchen, Paul G / Haslam, Stuart M / Mandal, Satadru Sekhar / Ganesh, N Vijaya / Bundle, David R / McGiven, John

Microorganisms

2022 Volume 10, Issue 4

Abstract: Brucellosis is a global disease and the world's most prevalent zoonosis. All cases in livestock and most cases in humans are caused by members of the ... ...

Abstract	Brucellosis is a global disease and the world's most prevalent zoonosis. All cases in livestock and most cases in humans are caused by members of the genus
Language	English
Publishing date	2022-03-25
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2720891-6
ISSN	2076-2607
ISSN	2076-2607
DOI	10.3390/microorganisms10040708
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Article ; Online: The Tip of Brucella O-Polysaccharide Is a Potent Epitope in Response to Brucellosis Infection and Enables Short Synthetic Antigens to Be Superior Diagnostic Reagents

Lucy Duncombe / Laurence Howells / Anna Haughey / Andrew V. Taylor / Daryan Kaveh / Sevil Erdenliğ Gϋrbilek / Anne Dell / Paul G. Hitchen / Stuart M. Haslam / Satadru Sekhar Mandal / N. Vijaya Ganesh / David R. Bundle / John McGiven

Microorganisms, Vol 10, Iss 708, p

2022 Volume 708

Abstract: Brucellosis is a global disease and the world’s most prevalent zoonosis. All cases in livestock and most cases in humans are caused by members of the genus Brucella that possess a surface O-polysaccharide (OPS) comprised of a rare monosaccharide 4-deoxy- ... ...

Abstract	Brucellosis is a global disease and the world’s most prevalent zoonosis. All cases in livestock and most cases in humans are caused by members of the genus Brucella that possess a surface O-polysaccharide (OPS) comprised of a rare monosaccharide 4-deoxy-4-formamido-D-mannopyranose assembled with α1,2 and α1,3 linkages. The OPS of the bacterium is the basis for serodiagnostic tests for brucellosis. Bacteria that also contain the same rare monosaccharide can induce antibodies that cross-react in serological tests. In previous work we established that synthetic oligosaccharides, representing elements of the Brucella A and M polysaccharide structures, were excellent antigens to explore the antibody response in the context of infection, immunisation and cross reaction. These studies suggested the existence of antibodies that are specific to the tip of the Brucella OPS. Sera from naturally and experimentally Brucella abortus -infected cattle as well as from cattle experimentally infected with the cross-reactive bacterium Yersinia enterocolitica O:9 and field sera that cross react in conventional serological assays were studied here with an expanded panel of synthetic antigens. The addition of chemical features to synthetic antigens that block antibody binding to the tip of the OPS dramatically reduced their polyclonal antibody binding capability providing conclusive evidence that the OPS tip (non-reducing end) is a potent epitope. Selected short oligosaccharides, including those that were exclusively α1,2 linked, also demonstrated superior specificity when evaluated with cross reactive sera compared to native smooth lipopolysaccharide (sLPS) antigen and capped native OPS. This surprising discovery suggests that the OPS tip epitope, even though common to both Brucella and Y. enterocolitica O:9, has more specific diagnostic properties than the linear portion of the native antigens. This finding opens the way to the development of improved serological tests for brucellosis.
Keywords	Brucella ; O-polysaccharide ; epitope ; Biology (General) ; QH301-705.5
Subject code	540
Language	English
Publishing date	2022-03-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
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Article: Bacterial glycoproteomics.

Hitchen, Paul G / Dell, Anne

Microbiology (Reading, England)

2005 Volume 152, Issue Pt 6, Page(s) 1575–1580

Abstract: Glycosylated proteins are ubiquitous components of eukaryote cellular surfaces, where the glycan moieties are implicated in a wide range of cell-cell recognition events. Once thought to be restricted to eukaryotes, glycosylation is now being increasingly ...

Abstract	Glycosylated proteins are ubiquitous components of eukaryote cellular surfaces, where the glycan moieties are implicated in a wide range of cell-cell recognition events. Once thought to be restricted to eukaryotes, glycosylation is now being increasingly reported in prokaryotes. Many of these discoveries have grown from advances in analytical technologies and genome sequencing. This review highlights the capabilities of high-sensitivity mass spectrometry for carbohydrate structure determination of bacterial glycoproteins and the emergence of glycoproteomic strategies that have evolved from proteomics and genomics for the functional analysis of bacterial glycosylation.
MeSH term(s)	Bacteria/chemistry ; Bacteria/metabolism ; Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Carbohydrate Sequence ; Glycoproteins/chemistry ; Glycosylation ; Mass Spectrometry ; Proteomics
Chemical Substances	Bacterial Proteins ; Glycoproteins
Language	English
Publishing date	2005-06-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1180712-x
ISSN	1465-2080 ; 1350-0872
ISSN (online)	1465-2080
ISSN	1350-0872
DOI	10.1099/mic.0.28859-0
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Article ; Online: Recombinant glycans on an S-layer self-assembly protein: a new dimension for nanopatterned biomaterials.

Steiner, Kerstin / Hanreich, Angelika / Kainz, Birgit / Hitchen, Paul G / Dell, Anne / Messner, Paul / Schäffer, Christina

Small (Weinheim an der Bergstrasse, Germany)

2014 Volume 4, Issue 10, Page(s) 1728–1740

Abstract: 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 ... ...

Abstract	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.
MeSH term(s)	Antigens, Bacterial/metabolism ; Bacterial Proteins/chemistry ; Bacterial Proteins/isolation & purification ; Bacterial Proteins/metabolism ; Biocompatible Materials/metabolism ; Campylobacter jejuni/metabolism ; Electrophoresis, Polyacrylamide Gel ; Escherichia coli/ultrastructure ; Genetic Engineering ; Geobacillus stearothermophilus/metabolism ; Glycoproteins/chemistry ; Glycoproteins/isolation & purification ; Glycoproteins/ultrastructure ; Glycosylation ; Models, Chemical ; Nanoparticles ; Periplasm/metabolism ; Polysaccharides/metabolism ; Polysaccharides, Bacterial/ultrastructure ; Protein Transport ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Chemical Substances	Antigens, Bacterial ; Bacterial Proteins ; Biocompatible Materials ; Glycoproteins ; Polysaccharides ; Polysaccharides, Bacterial
Language	English
Publishing date	2014-12-16
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2168935-0
ISSN	1613-6829 ; 1613-6810
ISSN (online)	1613-6829
ISSN	1613-6810
DOI	10.1002/smll.200701215
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Article ; Online: Z-band alternatively spliced PDZ motif protein (ZASP) is the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils.

Leung, Man-Ching / Hitchen, Paul G / Ward, Douglas G / Messer, Andrew E / Marston, Steven B

The Journal of biological chemistry

2012 Volume 288, Issue 7, Page(s) 4891–4898

Abstract: We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then ... ...

Abstract	We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc. All three methods showed that O-GlcNAc modification was predominantly in a group of bands ~90 kDa that did not correspond to any of the major myofibrillar proteins. MALDI-MS/MS identified the 90-kDa band as the protein ZASP (Z-band alternatively spliced PDZ motif protein), a minor component of the Z-disc (about 1 per 400 α-actinin) important for myofibrillar development and mechanotransduction. This was confirmed by the co-localization of O-GlcNAc and ZASP in Western blotting and by immunofluorescence microscopy. O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05). ZASP is only 22% of all O-GlcNAcylated proteins in mouse heart myofibrils.
MeSH term(s)	Acetylglucosamine/chemistry ; Adaptor Proteins, Signal Transducing/metabolism ; Adaptor Proteins, Signal Transducing/physiology ; Alternative Splicing ; Amino Acid Sequence ; Antibodies, Monoclonal/chemistry ; Fluorescent Antibody Technique, Indirect/methods ; Gene Expression Regulation ; Heart/physiology ; Humans ; LIM Domain Proteins/metabolism ; LIM Domain Proteins/physiology ; Microscopy, Fluorescence/methods ; Molecular Sequence Data ; Myofibrils/metabolism ; Peptides/chemistry ; Signal Transduction ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Chemical Substances	Adaptor Proteins, Signal Transducing ; Antibodies, Monoclonal ; LDB3 protein, human ; LIM Domain Proteins ; Peptides ; Acetylglucosamine (V956696549)
Language	English
Publishing date	2012-12-27
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M112.410316
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Article ; Online: Addressing Global Environmental Challenges to Mental Health Using Population Neuroscience: A Review.

Schumann, Gunter / Andreassen, Ole A / Banaschewski, Tobias / Calhoun, Vince D / Clinton, Nicholas / Desrivieres, Sylvane / Brandlistuen, Ragnhild Eek / Feng, Jianfeng / Hese, Soeren / Hitchen, Esther / Hoffmann, Per / Jia, Tianye / Jirsa, Viktor / Marquand, Andre F / Nees, Frauke / Nöthen, Markus M / Novarino, Gaia / Polemiti, Elli / Ralser, Markus /

Rapp, Michael / Schepanski, Kerstin / Schikowski, Tamara / Slater, Mel / Sommer, Peter / Stahl, Bernd Carsten / Thompson, Paul M / Twardziok, Sven / van der Meer, Dennis / Walter, Henrik / Westlye, Lars

JAMA psychiatry

2023 Volume 80, Issue 10, Page(s) 1066–1074

Abstract: Importance: Climate change, pollution, urbanization, socioeconomic inequality, and psychosocial effects of the COVID-19 pandemic have caused massive changes in environmental conditions that affect brain health during the life span, both on a population ... ...

Abstract	Importance: Climate change, pollution, urbanization, socioeconomic inequality, and psychosocial effects of the COVID-19 pandemic have caused massive changes in environmental conditions that affect brain health during the life span, both on a population level as well as on the level of the individual. How these environmental factors influence the brain, behavior, and mental illness is not well known. Observations: A research strategy enabling population neuroscience to contribute to identify brain mechanisms underlying environment-related mental illness by leveraging innovative enrichment tools for data federation, geospatial observation, climate and pollution measures, digital health, and novel data integration techniques is described. This strategy can inform innovative treatments that target causal cognitive and molecular mechanisms of mental illness related to the environment. An example is presented of the environMENTAL Project that is leveraging federated cohort data of over 1.5 million European citizens and patients enriched with deep phenotyping data from large-scale behavioral neuroimaging cohorts to identify brain mechanisms related to environmental adversity underlying symptoms of depression, anxiety, stress, and substance misuse. Conclusions and relevance: This research will lead to the development of objective biomarkers and evidence-based interventions that will significantly improve outcomes of environment-related mental illness.
MeSH term(s)	Humans ; Mental Health ; COVID-19/epidemiology ; Pandemics ; Anxiety Disorders ; Anxiety
Language	English
Publishing date	2023-08-23
Publishing country	United States
Document type	Review ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2701203-7
ISSN	2168-6238 ; 2168-622X
ISSN (online)	2168-6238
ISSN	2168-622X
DOI	10.1001/jamapsychiatry.2023.2996
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Article ; Online: Mass spectrometry in the analysis of N-linked and O-linked glycans.

North, Simon J / Hitchen, Paul G / Haslam, Stuart M / Dell, Anne

Current opinion in structural biology

2009 Volume 19, Issue 5, Page(s) 498–506

Abstract: Mass spectrometry (MS) continues to play a vital role in defining the structures of N-glycans and O-glycans in glycoproteins via glycomic and glycoproteomic methodologies. The former seeks to define the total N-glycan and/or O-glycan repertoire in a ... ...

Abstract	Mass spectrometry (MS) continues to play a vital role in defining the structures of N-glycans and O-glycans in glycoproteins via glycomic and glycoproteomic methodologies. The former seeks to define the total N-glycan and/or O-glycan repertoire in a biological sample whilst the latter is concerned with the analysis of glycopeptides. Recent technical developments have included improvements in tandem mass spectrometry (MS/MS and MS(n)) sequencing methodologies, more sensitive methods for analysing sulfated and polysialylated glycans and better procedures for defining the sites of O-glycosylation. New tools have been introduced to assist data handling and publicly accessible databases are being populated with glycomics data. Progress is exemplified by recent research in the fields of glycoimmunology, reproductive glycobiology, stem cells, bacterial glycosylation and non-mucin O-glycosylation.
MeSH term(s)	Animals ; Antigens/chemistry ; Antigens/immunology ; Glycomics ; Humans ; Mass Spectrometry/methods ; Polysaccharides/antagonists & inhibitors ; Polysaccharides/chemistry ; Polysaccharides/immunology ; Proteomics ; Stem Cells/chemistry
Chemical Substances	Antigens ; Polysaccharides
Language	English
Publishing date	2009-07-03
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1068353-7
ISSN	1879-033X ; 0959-440X
ISSN (online)	1879-033X
ISSN	0959-440X
DOI	10.1016/j.sbi.2009.05.005
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Article ; Online: Glycoproteomics: a powerful tool for characterizing the diverse glycoforms of bacterial pilins and flagellins.

Hitchen, Paul G / Twigger, Katie / Valiente, Esmeralda / Langdon, Rebecca H / Wren, Brendan W / Dell, Anne

Biochemical Society transactions

2011 Volume 38, Issue 5, Page(s) 1307–1313

Abstract: With glycosylation now firmly established across both Archaeal and bacterial proteins, a wide array of glycan diversity has become evident from structural analysis and genomic data. These discoveries have been built in part on the development and ... ...

Abstract	With glycosylation now firmly established across both Archaeal and bacterial proteins, a wide array of glycan diversity has become evident from structural analysis and genomic data. These discoveries have been built in part on the development and application of mass spectrometric technologies to the bacterial glycoproteome. This review highlights recent findings using high sensitivity MS of the large variation of glycans that have been reported on flagellin and pilin proteins of bacteria, using both 'top down' and 'bottom up' approaches to the characterization of these glycoproteins. We summarize current knowledge of the sugar modifications that have been observed on flagellins and pilins, in terms of both the diverse repertoire of monosaccharides observed, and the assemblage of moieties that decorate many of these sugars.
MeSH term(s)	Fimbriae Proteins/metabolism ; Flagellin/metabolism ; Glycoproteins/metabolism ; Glycosylation ; Mass Spectrometry ; Proteomics
Chemical Substances	Glycoproteins ; Flagellin (12777-81-0) ; Fimbriae Proteins (147680-16-8)
Language	English
Publishing date	2011-03-14
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	184237-7
ISSN	1470-8752 ; 0300-5127
ISSN (online)	1470-8752
ISSN	0300-5127
DOI	10.1042/BST0381307
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Article ; Online: N-glycosylation in Archaea: on the coordinated actions of Haloferax volcanii AglF and AglM.

Yurist-Doutsch, Sophie / Magidovich, Hilla / Ventura, Valeria V / Hitchen, Paul G / Dell, Anne / Eichler, Jerry

Molecular microbiology

2010 Volume 75, Issue 4, Page(s) 1047–1058

Abstract: Like Eukarya and Bacteria, Archaea are also capable of performing N-glycosylation. In the halophilic archaeon Haloferax volcanii, N-glycosylation is mediated by the products of the agl gene cluster. In the present report, this gene cluster was expanded ... ...

Abstract	Like Eukarya and Bacteria, Archaea are also capable of performing N-glycosylation. In the halophilic archaeon Haloferax volcanii, N-glycosylation is mediated by the products of the agl gene cluster. In the present report, this gene cluster was expanded to include an additional sequence, aglM, shown to participate in the biosynthesis of hexuronic acids contained within a pentasaccharide decorating the S-layer glycoprotein, a reporter H. volcanii glycoprotein. In response to different growth conditions, changes in the transcription profile of aglM mirrored changes in the transcription profiles of aglF, aglG and aglI, genes encoding confirmed participants in the H. volcanii N-glycosylation pathway, thus offering support to the hypothesis that in H. volcanii, N-glycosylation serves an adaptive role. Following purification, biochemical analysis revealed AglM to function as a UDP-glucose dehydrogenase. In a scoupled reaction with AglF, a previously identified glucose-1-phosphate uridyltransferase, UDP-glucuronic acid was generated from glucose-1-phosphate and UTP in a NAD(+)-dependent manner. These experiments thus represent the first step towards in vitro reconstitution of the archaeal N-glycosylation process.
MeSH term(s)	Archaeal Proteins/metabolism ; Glycoproteins/genetics ; Glycoproteins/metabolism ; Glycosylation ; Haloferax volcanii/genetics ; Haloferax volcanii/growth & development ; Haloferax volcanii/metabolism ; Multigene Family ; Transcription, Genetic
Chemical Substances	Archaeal Proteins ; Glycoproteins
Language	English
Publishing date	2010-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	619315-8
ISSN	1365-2958 ; 0950-382X
ISSN (online)	1365-2958
ISSN	0950-382X
DOI	10.1111/j.1365-2958.2009.07045.x
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Article ; Online: Glycoproteomic studies of IgE from a novel hyper IgE syndrome linked to PGM3 mutation.

Wu, Gang / Hitchen, Paul G / Panico, Maria / North, Simon J / Barbouche, Mohamed-Ridha / Binet, Daniel / Morris, Howard R / Dell, Anne / Haslam, Stuart M

Glycoconjugate journal

2015 Volume 33, Issue 3, Page(s) 447–456

Abstract: Glycans serve as important regulators of antibody activities and half-lives. IgE is the most heavily glycosylated antibody, but in comparison to other antibodies little is known about its glycan structure function relationships. We therefore describe the ...

Abstract	Glycans serve as important regulators of antibody activities and half-lives. IgE is the most heavily glycosylated antibody, but in comparison to other antibodies little is known about its glycan structure function relationships. We therefore describe the site specific IgE glycosylation from a patient with a novel hyper IgE syndrome linked to mutations in PGM3, which is an enzyme involved in synthesizing UDP-GlcNAc, a sugar donor widely required for glycosylation. A two-step method was developed to prepare two IgE samples from less than 1 mL of serum collected from a patient with PGM3 mutation and a patient with atopic dermatitis as a control subject. Then, a glycoproteomic strategy was used to study the site-specific glycosylation. No glycosylation was found at Asn264, whilst high mannose glycans were only detected at Asn275, tri-antennary glycans were exclusively observed at Asn99 and Asn252, and non-fucosylated complex glycans were detected at Asn99. The results showed similar glycosylation profiles between the two IgE samples. These observations, together with previous knowledge of IgE glycosylation, imply that IgE glycosylation is similarly regulated among healthy control, allergy and PGM3 related hyper IgE syndrome.
MeSH term(s)	Binding Sites ; Glycoproteins/chemistry ; Glycoproteins/metabolism ; Glycosylation ; Humans ; Immunoglobulin E/chemistry ; Immunoglobulin E/metabolism ; Job Syndrome/diagnosis ; Job Syndrome/genetics ; Job Syndrome/metabolism ; Mass Spectrometry/methods ; Molecular Diagnostic Techniques/methods ; Mutation ; Phosphoglucomutase/chemistry ; Phosphoglucomutase/genetics ; Phosphoglucomutase/metabolism ; Protein Processing, Post-Translational ; Proteome/chemistry ; Proteome/metabolism
Chemical Substances	Glycoproteins ; Proteome ; Immunoglobulin E (37341-29-0) ; PGM3 protein, human (EC 5.4.2.2) ; Phosphoglucomutase (EC 5.4.2.2)
Language	English
Publishing date	2015-12-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	283770-5
ISSN	1573-4986 ; 0282-0080
ISSN (online)	1573-4986
ISSN	0282-0080
DOI	10.1007/s10719-015-9638-y
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