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Journal articles on the topic 'Bacterial glycosylation'

Author: Grafiati

Published: 11 September 2021

Last updated: 30 July 2025

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1

Zhou, Meixian, and Hui Wu. "Glycosylation and biogenesis of a family of serine-rich bacterial adhesins." Microbiology 155, no. 2 (2009): 317–27. http://dx.doi.org/10.1099/mic.0.025221-0.

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Glycosylation of bacterial proteins is an important process for bacterial physiology and pathophysiology. Both O- and N-linked glycan moieties have been identified in bacterial glycoproteins. The N-linked glycosylation pathways are well established in Gram-negative bacteria. However, the O-linked glycosylation pathways are not well defined due to the complex nature of known O-linked glycoproteins in bacteria. In this review, we examine a new family of serine-rich O-linked glycoproteins which are represented by fimbriae-associated adhesin Fap1 of Streptococcus parasanguinis and human platelet-b

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Dell, Anne, Alaa Galadari, Federico Sastre, and Paul Hitchen. "Similarities and Differences in the Glycosylation Mechanisms in Prokaryotes and Eukaryotes." International Journal of Microbiology 2010 (2010): 1–14. http://dx.doi.org/10.1155/2010/148178.

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Recent years have witnessed a rapid growth in the number and diversity of prokaryotic proteins shown to carry N- and/or O-glycans, with protein glycosylation now considered as fundamental to the biology of these organisms as it is in eukaryotic systems. This article overviews the major glycosylation pathways that are known to exist in eukarya, bacteria and archaea. These are (i) oligosaccharyltransferase (OST)-mediated N-glycosylation which is abundant in eukarya and archaea, but is restricted to a limited range of bacteria; (ii) stepwise cytoplasmic N-glycosylation that has so far only been c

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Harding, Christian M., and Mario F. Feldman. "Glycoengineering bioconjugate vaccines, therapeutics, and diagnostics in E. coli." Glycobiology 29, no. 7 (2019): 519–29. http://dx.doi.org/10.1093/glycob/cwz031.

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Abstract The first, general glycosylation pathway in bacteria, the N-linked glycosylation system of Campylobacter jejuni, was discovered two decades ago. Since then, many diverse prokaryotic glycosylation systems have been characterized, including O-linked glycosylation systems that have no homologous counterparts in eukaryotic organisms. Shortly after these discoveries, glycosylation pathways were recombinantly introduced into E. coli creating the field of bacterial glycoengineering. Bacterial glycoengineering is an emerging biotechnological tool that harnesses prokaryotic glycosylation syste

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Chang, Te-Sheng, Jiumn-Yih Wu, Hsiou-Yu Ding, and Tzi-Yuan Wang. "Enzymatic Glycosylation of Ganoderma Terpenoid via Bacterial Glycosyltransferases and Glycoside Hydrolases." Biomolecules 15, no. 5 (2025): 655. https://doi.org/10.3390/biom15050655.

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Glycosylation is a critical enzymatic modification that involves the attachment of sugar moieties to target compounds, considerably influencing their physicochemical and biological characteristics. This review explored the role of two primary enzyme classes—glycosyltransferases (GTs) and glycoside hydrolases (GHs, glycosidases)—in catalyzing the glycosylation of natural products, with a specific focus on Ganoderma triterpenoids. While GTs typically use activated sugar donors, such as uridine diphosphate glucose, certain GHs can leverage more economical sugar sources, such as sucrose and starch

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Hitchen, Paul G., and Anne Dell. "Bacterial glycoproteomics." Microbiology 152, no. 6 (2006): 1575–80. http://dx.doi.org/10.1099/mic.0.28859-0.

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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 pro

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Sherlock, Orla, Ulrich Dobrindt, Jeppe B. Jensen, Rebecca Munk Vejborg, and Per Klemm. "Glycosylation of the Self-Recognizing Escherichia coli Ag43 Autotransporter Protein." Journal of Bacteriology 188, no. 5 (2006): 1798–807. http://dx.doi.org/10.1128/jb.188.5.1798-1807.2006.

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ABSTRACT Glycosylation is a common modulation of protein function in eukaryotes and is biologically important. However, in bacteria protein glycosylation is rare, and relatively few bacterial glycoproteins are known. In Escherichia coli only two glycoproteins have been described to date. Here we introduce a novel member to this exclusive group, namely, antigen 43 (Ag43), a self-recognizing autotransporter protein. By mass spectrometry Ag43 was demonstrated to be glycosylated by addition of heptose residues at several positions in the passenger domain. Glycosylation of Ag43 by the action of the

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Knudsen, Stine K., Allan Stensballe, Magnus Franzmann, Uffe B. Westergaard, and Daniel E. Otzen. "Effect of glycosylation on the extracellular domain of the Ag43 bacterial autotransporter: enhanced stability and reduced cellular aggregation." Biochemical Journal 412, no. 3 (2008): 563–77. http://dx.doi.org/10.1042/bj20071497.

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Autotransporters constitute the biggest group of secreted proteins in Gram-negative bacteria and contain a membrane-bound β-domain and a passenger domain secreted to the extracellular environment via an unusually long N-terminal sequence. Several passenger domains are known to be glycosylated by cytosolic glycosyl transferases, promoting bacterial attachment to mammalian cells. In the present study we describe the effect of glycosylation on the extracellular passenger domain of the Escherichia coli autotransporter Ag43α, which induces frizzy colony morphology and cell settling. We identify 16

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Fisher, Adam C., Charles H. Haitjema, Cassandra Guarino, et al. "Production of Secretory and Extracellular N-Linked Glycoproteins inEscherichia coli." Applied and Environmental Microbiology 77, no. 3 (2010): 871–81. http://dx.doi.org/10.1128/aem.01901-10.

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ABSTRACTTheCampylobacter jejuni pglgene cluster encodes a complete N-linked protein glycosylation pathway that can be functionally transferred intoEscherichia coli. In this system, we analyzed the interplay between N-linked glycosylation, membrane translocation and folding of acceptor proteins in bacteria. We developed a recombinant N-glycan acceptor peptide tag that permits N-linked glycosylation of diverse recombinant proteins expressed in the periplasm of glycosylation-competentE. colicells. With this “glycosylation tag,” a clear difference was observed in the glycosylation patterns found o

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9

Logan, Susan M. "Flagellar glycosylation – a new component of the motility repertoire?" Microbiology 152, no. 5 (2006): 1249–62. http://dx.doi.org/10.1099/mic.0.28735-0.

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The biosynthesis, assembly and regulation of the flagellar apparatus has been the subject of extensive studies over many decades, with considerable attention devoted to the peritrichous flagella of Escherichia coli and Salmonella enterica. The characterization of flagellar systems from many other bacterial species has revealed subtle yet distinct differences in composition, regulation and mode of assembly of this important subcellular structure. Glycosylation of the major structural protein, the flagellin, has been shown most recently to be an important component of numerous flagellar systems

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10

Szymanski, Christine M., and Brendan W. Wren. "Protein glycosylation in bacterial mucosal pathogens." Nature Reviews Microbiology 3, no. 3 (2005): 225–37. http://dx.doi.org/10.1038/nrmicro1100.

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Kelly, John, Harold Jarrell, Lorna Millar, et al. "Biosynthesis of the N-Linked Glycan in Campylobacter jejuni and Addition onto Protein through Block Transfer." Journal of Bacteriology 188, no. 7 (2006): 2427–34. http://dx.doi.org/10.1128/jb.188.7.2427-2434.2006.

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ABSTRACT In eukaryotes, N-linked protein glycosylation is a universal modification involving addition of preformed oligosaccharides to select Asn-Xaa-Ser/Thr motifs and influencing multiple biological events. We recently demonstrated that Campylobacter jejuni is the first member of the Bacteria to possess an N-linked glycan pathway. In this study, high-resolution magic angle spinning nuclear magnetic resonance (HR-MAS NMR) was applied to probe and quantitate C. jejuni N-glycan biosynthesis in vivo. To confirm HR-MAS NMR findings, glycosylation mutants were screened for chicken colonization pot

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Ahmad Izaham, Ameera Raudah, and Nichollas E. Scott. "Open Database Searching Enables the Identification and Comparison of Bacterial Glycoproteomes without Defining Glycan Compositions Prior to Searching." Molecular & Cellular Proteomics 19, no. 9 (2020): 1561–74. http://dx.doi.org/10.1074/mcp.tir120.002100.

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Mass spectrometry has become an indispensable tool for the characterization of glycosylation across biological systems. Our ability to generate rich fragmentation of glycopeptides has dramatically improved over the last decade yet our informatic approaches still lag behind. Although glycoproteomic informatics approaches using glycan databases have attracted considerable attention, database independent approaches have not. This has significantly limited high throughput studies of unusual or atypical glycosylation events such as those observed in bacteria. As such, computational approaches to ex

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Chattopadhyay, Aritra Nath, Mingdi Jiang, Jessa Marie V. Makabenta, Jungmi Park, Yingying Geng, and Vincent Rotello. "Nanosensor-Enabled Detection and Identification of Intracellular Bacterial Infections in Macrophages." Biosensors 14, no. 8 (2024): 360. http://dx.doi.org/10.3390/bios14080360.

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Opportunistic bacterial pathogens can evade the immune response by residing and reproducing within host immune cells, including macrophages. These intracellular infections provide reservoirs for pathogens that enhance the progression of infections and inhibit therapeutic strategies. Current sensing strategies for intracellular infections generally use immunosensing of specific biomarkers on the cell surface or polymerase chain reaction (PCR) of the corresponding nucleic acids, making detection difficult, time-consuming, and challenging to generalize. Intracellular infections can induce changes

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Irvine, Edward B., and Galit Alter. "Understanding the role of antibody glycosylation through the lens of severe viral and bacterial diseases." Glycobiology 30, no. 4 (2020): 241–53. http://dx.doi.org/10.1093/glycob/cwaa018.

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Abstract Abundant evidence points to a critical role for antibodies in protection and pathology across infectious diseases. While the antibody variable domain facilitates antibody binding and the blockade of infection, the constant domain (Fc) mediates cross talk with the innate immune system. The biological activity of the Fc region is controlled genetically via class switch recombination, resulting in the selection of distinct antibody isotypes and subclasses. However, a second modification is made to all antibodies, via post-translational changes in antibody glycosylation. Studies from auto

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Meireles, Diana, Rita Pombinho, Filipe Carvalho, Sandra Sousa, and Didier Cabanes. "Listeria monocytogenes Wall Teichoic Acid Glycosylation Promotes Surface Anchoring of Virulence Factors, Resistance to Antimicrobial Peptides, and Decreased Susceptibility to Antibiotics." Pathogens 9, no. 4 (2020): 290. http://dx.doi.org/10.3390/pathogens9040290.

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The cell wall of Listeria monocytogenes (Lm), a major intracellular foodborne bacterial pathogen, comprises a thick peptidoglycan layer that serves as a scaffold for glycopolymers such as wall teichoic acids (WTAs). WTAs contain non-essential sugar substituents whose absence prevents bacteriophage binding and impacts antigenicity, sensitivity to antimicrobials, and virulence. Here, we demonstrated, for the first time, the triple function of Lm WTA glycosylations in the following: (1) supporting the correct anchoring of major Lm virulence factors at the bacterial surface, namely Ami and InlB; (

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Olsen, O., and K. K. Thomsen. "Improvement of bacterial -glucanase thermostability by glycosylation." Journal of General Microbiology 137, no. 3 (1991): 579–85. http://dx.doi.org/10.1099/00221287-137-3-579.

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Nothaft, Harald, and Christine M. Szymanski. "Bacterial ProteinN-Glycosylation: New Perspectives and Applications." Journal of Biological Chemistry 288, no. 10 (2013): 6912–20. http://dx.doi.org/10.1074/jbc.r112.417857.

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Lujan, Agustin L., Diego O. Croci, Julián A. Gambarte Tudela, et al. "Glycosylation-dependent galectin–receptor interactions promoteChlamydia trachomatisinfection." Proceedings of the National Academy of Sciences 115, no. 26 (2018): E6000—E6009. http://dx.doi.org/10.1073/pnas.1802188115.

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Chlamydia trachomatis(Ct) constitutes the most prevalent sexually transmitted bacterium worldwide. Chlamydial infections can lead to severe clinical sequelae including pelvic inflammatory disease, ectopic pregnancy, and tubal infertility. As an obligate intracellular pathogen,Cthas evolved multiple strategies to promote adhesion and invasion of host cells, including those involving both bacterial and host glycans. Here, we show that galectin-1 (Gal1), an endogenous lectin widely expressed in female and male genital tracts, promotesCtinfection. Through glycosylation-dependent mechanisms involvi

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Chriswell, Meagan, Widian Jubair, Briana Tolbert, and Kristine Kuhn. "Bacterially-derived indole modulates murine arthritis through alteration of B cell glycosylation enzymes." Journal of Immunology 204, no. 1_Supplement (2020): 141.16. http://dx.doi.org/10.4049/jimmunol.204.supp.141.16.

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Abstract Indole, a bacteria-derived immunomodulatory metabolite that binds the aryl hydrocarbon receptor (AhR), is produced by bacterial tryptophanase in the intestinal tract of both mice and humans. Our studies using the murine collagen-induced arthritis (CIA) model of inflammatory arthritis demonstrated that intestinal bacteria influence disease severity through modulation of autoantibody glycosylation, and indole significantly correlated with the development of disease (P&lt;0.0001). Therefore, we hypothesized that indole modulates CIA through modulation of B cell glycosylation enzymes

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Ihssen, Julian, Jürgen Haas, Michael Kowarik, et al. "Increased efficiency of Campylobacter jejuni N -oligosaccharyltransferase PglB by structure-guided engineering." Open Biology 5, no. 4 (2015): 140227. http://dx.doi.org/10.1098/rsob.140227.

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Conjugate vaccines belong to the most efficient preventive measures against life-threatening bacterial infections. Functional expression of N -oligosaccharyltransferase ( N -OST) PglB of Campylobacter jejuni in Escherichia coli enables a simplified production of glycoconjugate vaccines in prokaryotic cells. Polysaccharide antigens of pathogenic bacteria can be covalently coupled to immunogenic acceptor proteins bearing engineered glycosylation sites. Transfer efficiency of PglB Cj is low for certain heterologous polysaccharide substrates. In this study, we increased glycosylation rates for Sal

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Zhu, Fan, Hua Zhang, and Hui Wu. "A Conserved Domain Is Crucial for Acceptor Substrate Binding in a Family of Glucosyltransferases." Journal of Bacteriology 197, no. 3 (2014): 510–17. http://dx.doi.org/10.1128/jb.02267-14.

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Serine-rich repeat glycoproteins (SRRPs) are highly conserved in streptococci and staphylococci. Glycosylation of SRRPs is important for bacterial adhesion and pathogenesis.Streptococcus agalactiaeis the leading cause of bacterial sepsis and meningitis among newborns. Srr2, an SRRP fromS. agalactiaestrain COH1, has been implicated in bacterial virulence. Four genes (gtfA,gtfB,gtfC, and gtfD) located downstream ofsrr2share significant homology with genes involved in glycosylation of other SRRPs. We have shown previously thatgtfAandgtfBencode two glycosyltransferases, GtfA and GtfB, that catalyz

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Prado Acosta, Mariano, and Bernd Lepenies. "Bacterial glycans and their interactions with lectins in the innate immune system." Biochemical Society Transactions 47, no. 6 (2019): 1569–79. http://dx.doi.org/10.1042/bst20170410.

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Bacterial surfaces are rich in glycoconjugates that are mainly present in their outer layers and are of great importance for their interaction with the host innate immune system. The innate immune system is the first barrier against infection and recognizes pathogens via conserved pattern recognition receptors (PRRs). Lectins expressed by innate immune cells represent an important class of PRRs characterized by their ability to recognize carbohydrates. Among lectins in innate immunity, there are three major classes including the galectins, siglecs, and C-type lectin receptors. These lectins ma

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Bhat, Aadil Hussain, Sudipa Maity, Kuldeep Giri, and Kiran Ambatipudi. "Protein glycosylation: Sweet or bitter for bacterial pathogens?" Critical Reviews in Microbiology 45, no. 1 (2019): 82–102. http://dx.doi.org/10.1080/1040841x.2018.1547681.

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Zhu, Fan, and Hui Wu. "Insights into bacterial protein glycosylation in human microbiota." Science China Life Sciences 59, no. 1 (2015): 11–18. http://dx.doi.org/10.1007/s11427-015-4980-7.

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Abu-Qarn, Mehtap, Assunta Giordano, Francesca Battaglia, et al. "Identification of AglE, a Second Glycosyltransferase Involved in N Glycosylation of the Haloferax volcanii S-Layer Glycoprotein." Journal of Bacteriology 190, no. 9 (2008): 3140–46. http://dx.doi.org/10.1128/jb.00056-08.

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ABSTRACT Archaea, like Eukarya and Bacteria, are able to N glycosylate select protein targets. However, in contrast to relatively advanced understanding of the eukaryal N glycosylation process and the information being amassed on the bacterial process, little is known of this posttranslational modification in Archaea. Toward remedying this situation, the present report continues ongoing efforts to identify components involved in the N glycosylation of the Haloferax volcanii S-layer glycoprotein. By combining gene deletion together with mass spectrometry, AglE, originally identified as a homolo

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Shi, Wei-Wei, Yong-Liang Jiang, Fan Zhu, Hui Wu, Cong-Zhao Zhou, and Yuxing Chen. "Structure of pneumococcal GtfA reveals a novel prokaryotic O-GlcNAc transferase." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C303. http://dx.doi.org/10.1107/s205327331409696x.

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Protein glycosylation is increasingly recognized as an important process for bacterial physiology and pathophysiology. Glycosylation of serine-rich repeat (SRR) glycoprotein PsrP is essential for the pathogenesis of Streptococcus pneumoniae, one of the most common human pathogens. This glycosylation process is initiated by a glycosyltransferase complex comprising two components, a core enzyme GtfA and a co-activator GtfB. Here we report the 2.0-Å crystal structure of GtfA in complex with GlcNAc and UDP. The structure possesses a core domain of GT-B fold and an unprecedented "add-on" domain of

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Bellavita, Rosa, Simone Braccia, Stefania Galdiero, and Annarita Falanga. "Glycosylation and Lipidation Strategies: Approaches for Improving Antimicrobial Peptide Efficacy." Pharmaceuticals 16, no. 3 (2023): 439. http://dx.doi.org/10.3390/ph16030439.

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Antimicrobial peptides (AMPs) have recently gained attention as a viable solution for combatting antibiotic resistance due to their numerous advantages, including their broad-spectrum activity, low propensity for inducing resistance, and low cytotoxicity. Unfortunately, their clinical application is limited due to their short half-life and susceptibility to proteolytic cleavage by serum proteases. Indeed, several chemical strategies, such as peptide cyclization, N-methylation, PEGylation, glycosylation, and lipidation, are widely used for overcoming these issues. This review describes how lipi

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Kreutzberger, Mark A. B., Cheryl Ewing, Frederic Poly, Fengbin Wang та Edward H. Egelman. "Atomic structure of theCampylobacter jejuniflagellar filament reveals how ε Proteobacteria escaped Toll-like receptor 5 surveillance". Proceedings of the National Academy of Sciences 117, № 29 (2020): 16985–91. http://dx.doi.org/10.1073/pnas.2010996117.

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Vertebrates, from zebra fish to humans, have an innate immune recognition of many bacterial flagellins. This involves a conserved eight-amino acid epitope in flagellin recognized by the Toll-like receptor 5 (TLR5). Several important human pathogens, such asHelicobacter pyloriandCampylobacter jejuni, have escaped TLR5 activation by mutations in this epitope. When such mutations were introduced intoSalmonellaflagellin, motility was abolished. It was previously argued, using very low-resolution cryoelectron microscopy (cryo-EM), thatC. jejuniaccommodated these mutations by forming filaments with

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Faridmoayer, Amirreza, Messele A. Fentabil, Dominic C. Mills, John S. Klassen, and Mario F. Feldman. "Functional Characterization of Bacterial Oligosaccharyltransferases Involved in O-Linked Protein Glycosylation." Journal of Bacteriology 189, no. 22 (2007): 8088–98. http://dx.doi.org/10.1128/jb.01318-07.

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ABSTRACT Protein glycosylation is an important posttranslational modification that occurs in all domains of life. Pilins, the structural components of type IV pili, are O glycosylated in Neisseria meningitidis, Neisseria gonorrhoeae, and some strains of Pseudomonas aeruginosa. In this work, we characterized the P. aeruginosa 1244 and N. meningitidis MC58 O glycosylation systems in Escherichia coli. In both cases, sugars are transferred en bloc by an oligosaccharyltransferase (OTase) named PglL in N. meningitidis and PilO in P. aeruginosa. We show that, like PilO, PglL has relaxed glycan specif

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Jervis, Adrian J., Rebecca Langdon, Paul Hitchen, et al. "Characterization of N-Linked Protein Glycosylation in Helicobacter pullorum." Journal of Bacteriology 192, no. 19 (2010): 5228–36. http://dx.doi.org/10.1128/jb.00211-10.

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ABSTRACT The first bacterial N-linked glycosylation system was discovered in Campylobacter jejuni, and the key enzyme involved in the coupling of glycan to asparagine residues within the acceptor sequon of the glycoprotein is the oligosaccharyltransferase PglB. Emerging genome sequence data have revealed that pglB orthologues are present in a subset of species from the Deltaproteobacteria and Epsilonproteobacteria, including three Helicobacter species: H. pullorum, H. canadensis, and H. winghamensis. In contrast to C. jejuni, in which a single pglB gene is located within a larger gene cluster

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Tytgat, Hanne L. P., Geert Schoofs, Jos Vanderleyden, et al. "Systematic Exploration of the Glycoproteome of the Beneficial Gut Isolate Lactobacillus rhamnosus GG." Journal of Molecular Microbiology and Biotechnology 26, no. 5 (2016): 345–58. http://dx.doi.org/10.1159/000447091.

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Glycoproteins form an interesting class of macromolecules involved in bacterial-host interactions, but they are not yet widely explored in Gram-positive and beneficial species. Here, an integrated and widely applicable approach was followed to identify putative bacterial glycoproteins, combining proteome fractionation with 2D protein and glycostained gels and lectin blots. This approach was validated for the microbiota isolate <i>Lactobacillus rhamnosus</i> GG. The approach resulted in a list of putative glycosylated proteins receiving a ‘glycosylation score'. Ultimately, we could

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Wyszyńska, Agnieszka, and Rafał Jabłuszewski. "PROTEIN GLYCOSYLATION IN BACTERIAL CELLS AND ITS POTENTIAL APPLICATIONS." Postępy Mikrobiologii - Advancements of Microbiology 60, no. 2 (2021): 137–49. http://dx.doi.org/10.21307/pm-2019.60.2.11.

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Tan, Felicia Y. Y., Christoph M. Tang, and Rachel M. Exley. "Sugar coating: bacterial protein glycosylation and host–microbe interactions." Trends in Biochemical Sciences 40, no. 7 (2015): 342–50. http://dx.doi.org/10.1016/j.tibs.2015.03.016.

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Kowarik, Michael, N. Martin Young, Shin Numao, et al. "Definition of the bacterial N-glycosylation site consensus sequence." EMBO Journal 25, no. 9 (2006): 1957–66. http://dx.doi.org/10.1038/sj.emboj.7601087.

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Ricciuto, Jessica, Susan R. Heimer, Michael S. Gilmore, and Pablo Argüeso. "Cell Surface O-Glycans Limit Staphylococcus aureus Adherence to Corneal Epithelial Cells." Infection and Immunity 76, no. 11 (2008): 5215–20. http://dx.doi.org/10.1128/iai.00708-08.

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ABSTRACT The mucin-rich environment of the intact corneal epithelium is thought to contribute to the prevention of Staphylococcus aureus infection. This study examined whether O-glycans, which constitute the majority of the mucin mass of epithelial cell glycocalyces, prevented bacterial adhesion and growth. Abrogation of mucin O glycosylation using the chemical primer benzyl-α-GalNAc resulted in increased adherence of parental strain RN6390 to apical human corneal-limbal epithelial (HCLE) cells and to biotinylated cell surface protein in static and liquid phase adhesion assays, consistent with

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Tzeng, Yih-Ling, Anup Datta, V. Kumar Kolli, Russell W. Carlson, and David S. Stephens. "Endotoxin of Neisseria meningitidis Composed Only of Intact Lipid A: Inactivation of the Meningococcal 3-Deoxy-d-Manno-Octulosonic Acid Transferase." Journal of Bacteriology 184, no. 9 (2002): 2379–88. http://dx.doi.org/10.1128/jb.184.9.2379-2388.2002.

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ABSTRACT Lipopolysaccharide, lipooligosaccharide (LOS), or endotoxin is important in bacterial survival and the pathogenesis of gram-negative bacteria. A necessary step in endotoxin biosynthesis is 3-deoxy-d-manno-octulosonic acid (Kdo) glycosylation of lipid A, catalyzed by the Kdo transferase KdtA (WaaA). In enteric gram-negative bacteria, this step is essential for survival. A nonpolar kdtA::aphA-3 mutation was created in Neisseria meningitidis via allelic exchange, and the mutant was viable. Detailed structural analysis demonstrated that the endotoxin of the kdtA::aphA-3 mutant was compose

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Chaban, Bonnie, Susan M. Logan, John F. Kelly, and Ken F. Jarrell. "AglC and AglK Are Involved in Biosynthesis and Attachment of Diacetylated Glucuronic Acid to the N-Glycan in Methanococcus voltae." Journal of Bacteriology 191, no. 1 (2008): 187–95. http://dx.doi.org/10.1128/jb.00885-08.

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ABSTRACT Recent advances in the field of prokaryotic N-glycosylation have established a foundation for the pathways and proteins involved in this important posttranslational protein modification process. To continue the study of the Methanococcus voltae N-glycosylation pathway, characteristics of known eukaryotic, bacterial, and archaeal proteins involved in the N-glycosylation process were examined and used to select candidate M. voltae genes for investigation as potential glycosyl transferase and flippase components. The targeted genes were knocked out via linear gene replacement, and the re

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Violetta, Marta Riva, Roberto Mazzoli, Cristina Barello, Paolo Fattori, Maria G. Giuffrida, and Enrica Pessione. "Combining LC-MS/MS, PMF and N-terminal amino acid sequencing for multiplexed characterization of a bacterial surfactant glycoprotein biosynthesized by Acinetobacter radioresistens S13." RSC Adv. 4, no. 21 (2014): 10918–27. http://dx.doi.org/10.1039/c4ra00692e.

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Wang, Mingqun, Yue Wang, Kaimeng Liu, et al. "Engineering a bacterial sialyltransferase for di-sialylation of a therapeutic antibody." Organic & Biomolecular Chemistry 18, no. 15 (2020): 2886–92. http://dx.doi.org/10.1039/d0ob00276c.

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A one-pot three-enzyme protocol was developed by engineering a bacterial sialyltransferase to facilitate the modification of therapeutic antibodies with N-acetylneuraminic acid or its derivatives towards optimized glycosylation.

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Alemka, Abofu, Harald Nothaft, Jing Zheng, and Christine M. Szymanski. "N-Glycosylation of Campylobacter jejuni Surface Proteins Promotes Bacterial Fitness." Infection and Immunity 81, no. 5 (2013): 1674–82. http://dx.doi.org/10.1128/iai.01370-12.

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ABSTRACTCampylobacter jejuniis the etiologic agent of human bacterial gastroenteritis worldwide. In contrast, despite heavy colonization,C. jejunimaintains a commensal mode of existence in chickens. The consumption of contaminated chicken products is thought to be the principal mode ofC. jejunitransmission to the human population.C. jejuniharbors a system for N-linked protein glycosylation that has been well characterized and modifies more than 60 periplasmic and membrane-bound proteins. However, the precise role of this modification in the biology ofC. jejuniremains unexplored. We hypothesize

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Jiang, Xiaosui, Warren G. Hill, Joseph M. Pilewski, and Ora A. Weisz. "Glycosylation differences between a cystic fibrosis and rescued airway cell line are not CFTR dependent." American Journal of Physiology-Lung Cellular and Molecular Physiology 273, no. 5 (1997): L913—L920. http://dx.doi.org/10.1152/ajplung.1997.273.5.l913.

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Altered glycosylation of mucus and membrane glycoconjugates could explain reported differences in binding of bacterial pathogens to cystic fibrosis (CF) versus normal tissue. However, because bacteria can alter cell surface glycoconjugates, it is not possible to assess the role of cystic fibrosis transmembrane conductance regulators (CFTR) in glycosylation in these studies. To address this issue, we have developed quantitative lectin binding assays to compare cell surface glycosylation in well-matched immortalized CF cells and rescued cell lines. The CF airway bronchial epithelial cell line IB

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Rezende, Samilla B., Karen G. N. Oshiro, Nelson G. O. Júnior, Octávio L. Franco, and Marlon H. Cardoso. "Advances on chemically modified antimicrobial peptides for generating peptide antibiotics." Chemical Communications 57, no. 88 (2021): 11578–90. http://dx.doi.org/10.1039/d1cc03793e.

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Chemical modifications in AMPs, including glycosylation, lipidation, PEGylation, cyclization, grafting, stapling, d-amino acids, and dendrimers are used to fine-tune peptide antibiotics candidates for bacterial infections treatment.

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Tvaroška, Igor. "The Role of Glycans in Human Immunity—A Sweet Code." Molecules 30, no. 13 (2025): 2678. https://doi.org/10.3390/molecules30132678.

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Glycans on the surface of all immune cells are the product of diverse post-translational modifications (glycosylation) that affect almost all proteins and possess enormous structural heterogeneity. Their bioinformational content is decoded by glycan-binding proteins (lectins, GBPs), such as C-type lectins, including selectins, galectins, and Siglecs. Glycans located on the surface of immune cells are involved in many immunological processes through interactions with GBPs. Lectins recognize changes in the glycan epitopes; distinguish among host (self), microbial (non-self), and tumor (modified

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Nagasawa, Yasuyuki, Taro Misaki, Seigo Ito, et al. "Title IgA Nephropathy and Oral Bacterial Species Related to Dental Caries and Periodontitis." International Journal of Molecular Sciences 23, no. 2 (2022): 725. http://dx.doi.org/10.3390/ijms23020725.

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A relationship between IgA nephropathy (IgAN) and bacterial infection has been suspected. As IgAN is a chronic disease, bacteria that could cause chronic infection in oral areas might be pathogenetic bacteria candidates. Oral bacterial species related to dental caries and periodontitis should be candidates because these bacteria are well known to be pathogenic in chronic dental disease. Recently, several reports have indicated that collagen-binding protein (cnm)-(+) Streptococcs mutans is relate to the incidence of IgAN and the progression of IgAN. Among periodontal bacteria, Treponema dentico

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Tian, Songhai, and Nini Zhou. "Gaining New Insights into Fundamental Biological Pathways by Bacterial Toxin-Based Genetic Screens." Bioengineering 10, no. 8 (2023): 884. http://dx.doi.org/10.3390/bioengineering10080884.

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Genetic screen technology has been applied to study the mechanism of action of bacterial toxins—a special class of virulence factors that contribute to the pathogenesis caused by bacterial infections. These screens aim to identify host factors that directly or indirectly facilitate toxin intoxication. Additionally, specific properties of certain toxins, such as membrane interaction, retrograde trafficking, and carbohydrate binding, provide robust probes to comprehensively investigate the lipid biosynthesis, membrane vesicle transport, and glycosylation pathways, respectively. This review speci

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Hitchen, Paul G., Katie Twigger, Esmeralda Valiente, Rebecca H. Langdon, Brendan W. Wren, and Anne Dell. "Glycoproteomics: a powerful tool for characterizing the diverse glycoforms of bacterial pilins and flagellins." Biochemical Society Transactions 38, no. 5 (2010): 1307–13. http://dx.doi.org/10.1042/bst0381307.

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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 summar

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Mann, Evan, and Chris Whitfield. "A widespread three-component mechanism for the periplasmic modification of bacterial glycoconjugates." Canadian Journal of Chemistry 94, no. 11 (2016): 883–93. http://dx.doi.org/10.1139/cjc-2015-0594.

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The diverse structures of bacterial glycoconjugates are generally established during the early stages of synthesis by the activities of nucleotide sugar-dependent glycosyltransferases active in the cytoplasm. However, in some cases, further modifications of varying complexity occur after the glycoconjugate is exported to the periplasm. These processes are distinguished by the involvement of polyprenyl monosphosphoryl donors and require glycosyltransferases possessing GT-C folds. Established prototypes are found in modifications of some bacterial lipopolysaccharides, where 4-amino-4-deoxy-l-ara

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Yao, Hao, Guo Li, Xianglian Xiong, et al. "LygA retention on the surface of Listeria monocytogenes via its interaction with wall teichoic acid modulates bacterial homeostasis and virulence." PLOS Pathogens 19, no. 6 (2023): e1011482. http://dx.doi.org/10.1371/journal.ppat.1011482.

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Wall teichoic acid (WTA) is the abundant cell wall-associated glycopolymer in Gram-positive bacteria, playing crucial roles in surface proteins retention, bacterial homeostasis, and virulence. Hypervirulent serovar (SV) 4h Listeria monocytogenes is a newly designated serotype with only galactosylated (Gal) type II WTA. Although the surface association of some proteins relies on the WTA glycosylation, the nature and function of the noncovalent interactions between cell wall-associated proteins and WTA are less known. In this study, we found Gal-WTA plays a key role in modulating the novel glyci

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Ní Cheallaigh, Aisling, and Stefan Oscarson. "Synthesis of building blocks for an iterative approach towards oligomers of the Streptococcus pneumoniae type 1 zwitterionic capsular polysaccharide repeating unit." Canadian Journal of Chemistry 94, no. 11 (2016): 940–60. http://dx.doi.org/10.1139/cjc-2016-0006.

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Zwitterionic capsular polysaccharide extracts, ∼8 kDa in mass, from Streptococcus pneumoniae type 1 (Spt1) have shown unique T-cell activating properties. Oligomers of the trisaccharide repeating unit of the Spt1 capsular polysaccharide [→3)-4-NH2-α-d-QuipNAc-(1→4)-α-d-GalpA-(1→3)-α-d-GalpA-(1-]n of defined length are needed to further investigate this response. An approach towards iteratively extendable trisaccharide building blocks of the zwitterionic capsular polysaccharides of Spt1 is described. Key elements include the comparison of pre-glycosylation oxidation and post-glycosylation oxida

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Wu, Ren, Meixian Zhou, and Hui Wu. "Purification and Characterization of an Active N-Acetylglucosaminyltransferase Enzyme Complex from Streptococci." Applied and Environmental Microbiology 76, no. 24 (2010): 7966–71. http://dx.doi.org/10.1128/aem.01434-10.

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ABSTRACT A new family of bacterial serine-rich repeat glycoproteins can function as adhesins required for biofilm formation and pathogenesis in streptococci and staphylococci. Biogenesis of these proteins depends on a gene cluster coding for glycosyltransferases and accessory secretion proteins. Previous studies show that Fap1, a member of this family from Streptococcus parasanguinis, can be glycosylated by a protein glycosylation complex in a recombinant heterogeneous host. Here we report a tandem affinity purification (TAP) approach used to isolate and study protein complexes from native str

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