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Journal articles on the topic 'Glycoproteins Biotechnology'

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Author: Grafiati

Published: 10 December 2022

Last updated: 29 January 2023

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1

Zhao, Wenzhu, Ge Xu, Yuejiao Chen, Zhipeng Yu, Jianrong Li, Hanjie Yu, and Xiaojun Liao. "Glycan characterisation and antioxidant activity of a novel N-linked glycoprotein from okra." International Food Research Journal 28, no. 6 (December 1, 2021): 1119–30. http://dx.doi.org/10.47836/ifrj.28.6.03.

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Glycoproteins are present in all living beings, and have many biological functions. The characterisation of glycan structures of plant glycoproteins has become increasingly important in biotechnology and agricultural applications. In the present work, the antioxidant activities of the okra glycoprotein were assessed. The glycan structures of the okra glycoprotein were analysed using lectin microarray combined with matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry. The okra glycoprotein showed relatively strong 2,2-diphenyl-1-picrylhydrazyl-scavenging ability and reducing power. In addition, the glycan structures of the okra glycoprotein mainly contained N-acetylglucosamine, mannose, and galactose. Furthermore, complex-type N-glycans were the major type of glycan structures from the okra glycoprotein. Most of the complex N-glycans of the okra glycoprotein had terminal GalNAc and Gal N-glycan structures; the glycoprotein showed a high level of fucosylated complex-type glycans. Therefore, the okra glycoprotein is a promising antioxidant. Results of the present work might serve as a reference for a better understanding of the structural information and bioactivity of okra glycoprotein.

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2

Hsieh–Wilson, Linda C. "Tailor-made glycoproteins." Trends in Biotechnology 22, no. 10 (October 2004): 489–91. http://dx.doi.org/10.1016/j.tibtech.2004.08.009.

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3

Mellors, Alan, and D. Robert Sutherland. "Tools to cleave glycoproteins." Trends in Biotechnology 12, no. 1 (January 1994): 15–18. http://dx.doi.org/10.1016/0167-7799(94)90006-x.

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4

Lepenies, Bernd, and Peter H. Seeberger. "Simply better glycoproteins." Nature Biotechnology 32, no. 5 (May 2014): 443–45. http://dx.doi.org/10.1038/nbt.2893.

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5

Goochee, Charles F., Michael J. Gramer, Dana C. Andersen, Jennifer B. Bahr, and James R. Rasmussen. "The Oligosaccharides of Glycoproteins: Bioprocess Factors Affecting Oligosaccharide Structure and their Effect on Glycoprotein Properties." Bio/Technology 9, no. 12 (December 1991): 1347–55. http://dx.doi.org/10.1038/nbt1291-1347.

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6

Calo, Doron, Yael Eilam, Rachel G. Lichtenstein, and Jerry Eichler. "Towards Glycoengineering in Archaea: Replacement of Haloferax volcanii AglD with Homologous Glycosyltransferases from Other Halophilic Archaea." Applied and Environmental Microbiology 76, no. 17 (July 2, 2010): 5684–92. http://dx.doi.org/10.1128/aem.00681-10.

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ABSTRACT Like eukarya and bacteria, archaea also perform N-glycosylation. However, the N-linked glycans of archaeal glycoproteins present a variety not seen elsewhere. Archaea accordingly rely on N-glycosylation pathways likely involving a broad range of species-specific enzymes. To harness the enormous applied potential of such diversity for the generation of glycoproteins bearing tailored N-linked glycans, the development of an appropriate archaeal glycoengineering platform is required. With a sequenced genome, a relatively well-defined N-glycosylation pathway, and molecular tools for gene manipulation, the haloarchaeon Haloferax volcanii (Hfx. volcanii) represents a promising candidate. Accordingly, cells lacking AglD, a glycosyltransferase involved in adding the final hexose of a pentasaccharide N-linked to the surface (S)-layer glycoprotein, were transformed to express AglD homologues from other haloarchaea. The introduction of nonnative versions of AglD led to the appearance of an S-layer glycoprotein similar to the protein from the native strain. Indeed, mass spectrometry confirmed that AglD and its homologues introduce the final hexose to the N-linked S-layer glycoprotein pentasaccharide. Heterologously expressed haloarchaeal AglD homologues contributed to N-glycosylation in Hfx. volcanii despite an apparent lack of AglD function in those haloarchaea from where the introduced homologues came. For example, although functional in Hfx. volcanii, no transcription of the Halobacterium salinarum aglD homologue, OE1482, was detected in cells of the native host grown under various conditions. Thus, at least one AglD homologue works more readily in Hfx. volcanii than in the native host. These results warrant the continued assessment of Hfx. volcanii as a glycosylation “workshop.”

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7

Manocha, M. S., D. Xiong, and V. Govindsamy. "Isolation and partial characterization of a complementary protein from the mycoparasite Piptocephalis virginiana that specifically binds to two glycoproteins at the host cell surface." Canadian Journal of Microbiology 43, no. 7 (July 1, 1997): 625–32. http://dx.doi.org/10.1139/m97-089.

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Immunofluorescence microscopy was used to detect in the mycoparasite Piptocephalis virginiana the presence of a complementary glycoprotein that binds specifically to the host cell surface glycoproteins b and c, reported earlier from our laboratory. Germinated spores of P. virginiana treated with cell wall extract of the host Mortierella pusilla, primary antibody prepared against cell wall glycoproteins b and c, and fluorescein isothiocyanate (FITC) – goat anti-rabbit IgG conjugate showed fluorescence. Immunobinding analysis identified from the mycoparasite a protein of 100 kDa that binds with the host glycoproteins b and c, separately as well as collectively. Its purification was achieved by (i) 60% ammonium sulfate precipitation, (ii) heat treatment, (iii) Sephadex G-100 gel filtration, and (iv) preparative polyacrylamide gel electrophoresis (PAGE). The purity was ascertained by sodium dodecyl sulphate (SDS) – PAGE and Western blot analysis. Positive reaction to periodic acid – Schiff s reagent revealed its glycoprotein nature, and mannose was identified as a major sugar component. The specificity of the polyclonal antibody raised against electrophoretically purified complementary protein in rabbit was confirmed by dot immunobinding and Western blot analyses. Immunofluorescence microscopy revealed surface localization of the protein on the germ tubes of P. virginiana. Fluorescence was also observed at the surface of the germinated spores and hyphae of the host M. pusilla, after treatment with complementary protein from P. virginiana, primary antibody prepared against the complementary protein, and FITC – goat anti-rabbit IgG conjugate.Key words: biotrophic mycoparasite, cell surface agglutinin, glycoprotein immunobinding, immunofluorescence, mucoraceous host.

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8

Shirai, Sahoko, Ryota Uemura, Megumi Maeda, Hiroyuki Kajiura, Ryo Misaki, Kazuhito Fujiyama, and Yoshinobu Kimura. "Direct evidence of cytosolic PNGase activity in Arabidopsis thaliana: in vitro assay system for plant cPNGase activity." Bioscience, Biotechnology, and Biochemistry 85, no. 6 (March 16, 2021): 1460–63. http://dx.doi.org/10.1093/bbb/zbab047.

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ABSTRACT Cytosolic peptide:N-glycanase (cPNGase), which occurs ubiquitously in eukaryotic cells, is involved in the de-N-glycosylation of misfolded glycoproteins in the protein quality control system. In this study, we aimed to provide direct evidence of plant cPNGase activity against a denatured glycoprotein using a crude extract prepared from a mutant line of Arabidopsis thaliana lacking 2 acidic PNGase genes.

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9

Berman, Phillip W., and Laurence A. Lasky. "Engineering glycoproteins for use as pharmaceuticals." Trends in Biotechnology 3, no. 2 (February 1985): 51–53. http://dx.doi.org/10.1016/0167-7799(85)90059-9.

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10

Manocha, M. S., and Y. Chen. "Isolation and partial characterization of host cell surface agglutinin and its role in attachment of a biotrophic mycoparasite." Canadian Journal of Microbiology 37, no. 5 (May 1, 1991): 377–83. http://dx.doi.org/10.1139/m91-061.

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Cell surface proteins obtained by alkaline extraction from isolated cell walls of Mortierella pusilla and M. candelabrum, host and nonhost, respectively, of the mycoparasite Piptocephalis virginiana, were tested for their ability to agglutinate mycoparasite spores. The host cell wall protein extract had a high agglutinating activity (788 agglutination units/mg) compared with that of the nonhost extract (21 agglutination units/mg). Sodium dodecyl sulfate – polyacrylamide gel electrophoresis of the crude extract of the host revealed four bands, a, b, c, and d, with respective Mr of 117 000, 100 000, 85 000 and 64 000; these bands except for a faint band c, were absent from the nonhost surface. Deletion of proteins b or c from the crude protein extract of the host significantly reduced its agglutinating activity. Proteins b and c, purified by a series of procedures, were shown to be glycoproteins with glucose and N-acetylglucosamine as major saccharides. The agglutinating activity of a mixture of pure proteins b and c was over 500 times that of either glycoprotein alone, suggesting an involvement of both glycoproteins in the agglutination process. Further characterization showed that the two glycoproteins were heat-resistant with respect to their agglutinin function, which could be totally inhibited by three sugars: arabinose, glucose and N-acetyglucosamine. It is suggested that glycoproteins b and c are the two subunits of a carbohydrate-binding agglutinin present at the host cell surface and involved in agglutination and attachment of the mycoparasite germ tubes. Key words: agglutinin, attachment, cell surface, sugars, glycoproteins, mycoparasitism.

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11

Hassan, Sammer-ul, Ahmed Donia, Usman Sial, Xunli Zhang, and Habib Bokhari. "Glycoprotein- and Lectin-Based Approaches for Detection of Pathogens." Pathogens 9, no. 9 (August 24, 2020): 694. http://dx.doi.org/10.3390/pathogens9090694.

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Infectious diseases alone are estimated to result in approximately 40% of the 50 million total annual deaths globally. The importance of basic research in the control of emerging and re-emerging diseases cannot be overemphasized. However, new nanotechnology-based methodologies exploiting unique surface-located glycoproteins or their patterns can be exploited to detect pathogens at the point of use or on-site with high specificity and sensitivity. These technologies will, therefore, affect our ability in the future to more accurately assess risk. The critical challenge is making these new methodologies cost-effective, as well as simple to use, for the diagnostics industry and public healthcare providers. Miniaturization of biochemical assays in lab-on-a-chip devices has emerged as a promising tool. Miniaturization has the potential to shape modern biotechnology and how point-of-care testing of infectious diseases will be performed by developing smart microdevices that require minute amounts of sample and reagents and are cost-effective, robust, and sensitive and specific. The current review provides a short overview of some of the futuristic approaches using simple molecular interactions between glycoproteins and glycoprotein-binding molecules for the efficient and rapid detection of various pathogens at the point of use, advancing the emerging field of glyconanodiagnostics.

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12

Werner, Anselm, Rüdiger Horstkorte, Dagobert Glanz, Karina Biskup, Véronique Blanchard, Markus Berger, and Kaya Bork. "Glycoengineering the N-acyl side chain of sialic acid of human erythropoietin affects its resistance to sialidase." Biological Chemistry 393, no. 8 (August 1, 2012): 777–83. http://dx.doi.org/10.1515/hsz-2012-0138.

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Abstract During the last years, the use of therapeutic glycoproteins has increased strikingly. Glycosylation of recombinant glycoproteins is of major importance in biotechnology, as the glycan composition of recombinant glycoproteins impacts their pharmacological properties. The terminal position of N-linked complex glycans in mammals is typically occupied by sialic acid. The presence of sialic acid is crucial for functionality and affects the half-life of glycoproteins. However, glycoproteins in the bloodstream become desialylated over time and are recognized by the asialoglycoprotein receptors via the exposed galactose and targeted for degradation. Non-natural sialic acid precursors can be used to engineer the glycosylation side chains by biochemically introducing new non-natural terminal sialic acids. Previously, we demonstrated that the physiological precursor of sialic acid (i.e., N-acetylmannosamine) can be substituted by the non-natural precursors N-propanoylmannosamine (ManNProp) or N-pentanoylmannosamine (ManNPent) by their simple application to the cell culture medium. Here, we analyzed the glycosylation of erythropoietin (EPO). By feeding cells with ManNProp or ManNPent, we were able to incorporate N-propanoyl or N-pentanoyl sialic acid in significant amounts into EPO. Using a degradation assay with sialidase, we observed a higher resistance of EPO to sialidase after incorporation of N-propanoyl or N-pentanoyl sialic acid.

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13

Schmidt, Brigitte, Urs Heimgartner, Branko Kozulić, and Matti S. A. Leisola. "Lignin peroxidases are oligomannose type glycoproteins." Journal of Biotechnology 13, no. 2-3 (February 1990): 223–28. http://dx.doi.org/10.1016/0168-1656(90)90107-m.

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14

Fujise, Hiroshi, Shigemi Sasawatari, Takeshi Annoura, Teruo Ikeda, and Kazumitsu Ueda. "3,3′,4,4′,5-Pentachlorobiphenyl Inhibits Drug Efflux Through P-Glycoprotein in KB-3 Cells Expressing Mutant Human P-Glycoprotein." Journal of Biomedicine and Biotechnology 2004, no. 3 (2004): 137–42. http://dx.doi.org/10.1155/s1110724304308028.

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The effects on the drug efflux of3,3′,4,4′,5-pentachlorobiphenyl (PCB-126), the most toxic of all coplanar polychlorinated biphenyls (Co-PCBs), were examined in KB-3 cells expressing human wild-type and mutant P-glycoprotein in which the 61st amino acid was substituted for serine or phenylalanine (KB3-Phe61). In the cells expressing P-glycoproteins, accumulations of vinblastine and colchicine decreased form 85% to 92% and from 62% to 91%, respectively, and the drug tolerances for these chemicals were increased. InKB3-Phe61, the decreases in drug accumulation were inhibited by adding PCB-126 in a way similar to that with cyclosporine A: by adding 1μM PCB-126, the accumulations of vinblastine and colchicine increased up to 3.3- and 2.3-fold, respectively. It is suggested that PCB-126 decreased the drug efflux by inhibiting the P-glycoprotein inKB3-Phe61. Since there were various P-glycoproteins and many congeners of Co-PCBs, this inhibition has to be considered a new cause of the toxic effects of Co-PCBs.

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15

Tytgat, Hanne L. P., Geert Schoofs, Jos Vanderleyden, Els J. M. Van Damme, Ruddy Wattiez, Sarah Lebeer, and Baptiste Leroy. "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 identify 41 unique glycosylated proteins in <i>L. rhamnosus</i> GG (6 top-confidence, 10 high-confidence and 25 putative hits; classification based on glycosylation score). Most glycoproteins are associated with the cell wall and membrane. Identified glycoproteins include proteins involved in transport, translation, and sugar metabolism processes. A robust screening resulted in a comprehensive mapping of glycoproteins in <i>L. rhamnosus</i> GG. Our results reflect the glycosylation of sugar metabolism enzymes, transporters, and other proteins crucial for cell physiology. We hypothesize that protein glycosylation can confer an extra level of regulation, for example by affecting enzyme functions. This is the first systematic study of the glycoproteome of a probiotic and beneficial gut isolate.

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16

Parekh, Raj B., and Thakor P. Patel. "Comparing the glycosylation patterns of recombinant glycoproteins." Trends in Biotechnology 10 (1992): 276–80. http://dx.doi.org/10.1016/0167-7799(92)90244-p.

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17

PAREKH, R. "N-glycosylation and the production of recombinant glycoproteins." Trends in Biotechnology 7, no. 5 (May 1989): 117–22. http://dx.doi.org/10.1016/0167-7799(89)90087-5.

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18

Chang, Kern Hee, Tamao Endo, and Jung Hoe Kim. "Quantitative analysis of oligosaccharide structure of glycoproteins." Biotechnology and Bioprocess Engineering 5, no. 2 (April 2000): 136–40. http://dx.doi.org/10.1007/bf02931885.

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19

Lee, K. B., D. Loganathan, Z. M. Merchant, and R. J. Linhardt. "Carbohydrate analysis of glycoproteins A review." Applied Biochemistry and Biotechnology 23, no. 1 (January 1990): 53–80. http://dx.doi.org/10.1007/bf02942052.

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20

Vallbracht, Melina, Barbara G. Klupp, and Thomas C. Mettenleiter. "Die komplexe Fusionsmaschinerie der Herpesviren." BIOspektrum 28, no. 2 (March 2022): 168–70. http://dx.doi.org/10.1007/s12268-022-1718-5.

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AbstractEnveloped viruses enter cells by fusion between viral and cellular membranes which is catalyzed by specialized fusogenic glycoproteins (g) on the viral surface. Many viruses use a single fusion protein for entry. In contrast, herpesviruses depend on a complex fusion machinery. Here, we discuss the role of the individual herpesvirus fusion machinery components and answer two basic questions: why does the herpesvirus fusion protein gB depend on other glycoproteins for fusion, and can gB be transformed to function autonomously?

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21

Song, Yunkyoung, Min Hee Choi, Jeong-Nam Park, Moo Woong Kim, Eun Jung Kim, Hyun Ah Kang, and Jeong-Yoon Kim. "Engineering of the Yeast Yarrowia lipolytica for the Production of Glycoproteins Lacking the Outer-Chain Mannose Residues of N-Glycans." Applied and Environmental Microbiology 73, no. 14 (May 18, 2007): 4446–54. http://dx.doi.org/10.1128/aem.02058-06.

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ABSTRACT In an attempt to engineer a Yarrowia lipolytica strain to produce glycoproteins lacking the outer-chain mannose residues of N-linked oligosaccharides, we investigated the functions of the OCH1 gene encoding a putative α-1,6-mannosyltransferase in Y. lipolytica. The complementation of the Saccharomyces cerevisiae och1 mutation by the expression of YlOCH1 and the lack of in vitro α-1,6-mannosyltransferase activity in the Yloch1 null mutant indicated that YlOCH1 is a functional ortholog of S. cerevisiae OCH1. The oligosaccharides assembled on two secretory glycoproteins, the Trichoderma reesei endoglucanase I and the endogenous Y. lipolytica lipase, from the Yloch1 null mutant contained a single predominant species, the core oligosaccharide Man8GlcNAc2, whereas those from the wild-type strain consisted of oligosaccharides with heterogeneous sizes, Man8GlcNAc2 to Man12GlcNAc2. Digestion with α-1,2- and α-1,6-mannosidase of the oligosaccharides from the wild-type and Yloch1 mutant strains strongly supported the possibility that the Yloch1 mutant strain has a defect in adding the first α-1,6-linked mannose to the core oligosaccharide. Taken together, these results indicate that YlOCH1 plays a key role in the outer-chain mannosylation of N-linked oligosaccharides in Y. lipolytica. Therefore, the Yloch1 mutant strain can be used as a host to produce glycoproteins lacking the outer-chain mannoses and further developed for the production of therapeutic glycoproteins containing human-compatible oligosaccharides.

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22

Aronson, Nathan N., and Michael J. Kuranda. "Lysosomal degradation of Asn‐linked glycoproteins." FASEB Journal 3, no. 14 (December 1989): 2615–22. http://dx.doi.org/10.1096/fasebj.3.14.2531691.

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23

Vervecken, Wouter, Vladimir Kaigorodov, Nico Callewaert, Steven Geysens, Kristof De Vusser, and Roland Contreras. "In Vivo Synthesis of Mammalian-Like, Hybrid-Type N-Glycans in Pichia pastoris." Applied and Environmental Microbiology 70, no. 5 (May 2004): 2639–46. http://dx.doi.org/10.1128/aem.70.5.2639-2646.2004.

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ABSTRACT The Pichia pastoris N-glycosylation pathway is only partially homologous to the pathway in human cells. In the Golgi apparatus, human cells synthesize complex oligosaccharides, whereas Pichia cells form mannose structures that can contain up to 40 mannose residues. This hypermannosylation of secreted glycoproteins hampers the downstream processing of heterologously expressed glycoproteins and leads to the production of protein-based therapeutic agents that are rapidly cleared from the blood because of the presence of terminal mannose residues. Here, we describe engineering of the P. pastoris N-glycosylation pathway to produce nonhyperglycosylated hybrid glycans. This was accomplished by inactivation of OCH1 and overexpression of an α-1,2-mannosidase retained in the endoplasmic reticulum and N-acetylglucosaminyltransferase I and β-1,4-galactosyltransferase retained in the Golgi apparatus. The engineered strain synthesized a nonsialylated hybrid-type N-linked oligosaccharide structure on its glycoproteins. The procedures which we developed allow glycan engineering of any P. pastoris expression strain and can yield up to 90% homogeneous protein-linked oligosaccharides.

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24

MISAKI, Ryo, Yoshinobu KIMURA, Kazuhito FUJIYAMA, and Tatsuji SEKI. "Glycoproteins Secreted from Suspension-cultured Tobacco BY2 Cells have Distinct Glycan Structures from Intracellular Glycoproteins." Bioscience, Biotechnology, and Biochemistry 65, no. 11 (January 2001): 2482–88. http://dx.doi.org/10.1271/bbb.65.2482.

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25

Sedzik, Jan, Keiichi Uyemura, and Tomitake Tsukihara. "Towards crystallization of hydrophobic myelin glycoproteins: P0 and PASII/PMP22." Protein Expression and Purification 26, no. 3 (December 2002): 368–77. http://dx.doi.org/10.1016/s1046-5928(02)00564-8.

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26

Wyss, Daniel F., and Gerhard Wagner. "The structural role of sugars in glycoproteins." Current Opinion in Biotechnology 7, no. 4 (August 1996): 409–16. http://dx.doi.org/10.1016/s0958-1669(96)80116-9.

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27

MORRIS, H. "Mass spectrometry of natural and recombinant proteins and glycoproteins." Trends in Biotechnology 6, no. 7 (July 1988): 140–47. http://dx.doi.org/10.1016/0167-7799(88)90083-2.

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28

Park, Yong-Il, Byung-Dae Yoon, and Yuan Chuan Lee. "Sialic acids inTrichoplusia ni andDanaus plexippus egg glycoproteins." Biotechnology and Bioprocess Engineering 4, no. 3 (October 1999): 165–69. http://dx.doi.org/10.1007/bf02931922.

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29

Deregt, Dirk, Saad A. Masri, Hyun J. Cho, and Helle Bielefeldt Ohmann. "Bovine viral diarrhea virus proteins: relatedness of p175 with p80 and p125 and evidence of glycoprotein processing." Canadian Journal of Microbiology 37, no. 11 (November 1, 1991): 815–22. http://dx.doi.org/10.1139/m91-141.

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Three monoclonal antibodies, which recognized two nonoverlapping antigenic domains and were reactive to the bovine viral diarrhea virus (BVDV) p80 protein, were found to cross react with the p125 protein of both cytopathic and noncytopathic BVDVs and a molecular weight 175 000 BVDV protein (p175). Results from limited proteolysis and chemical cleavage experiments confirmed the relatedness of these three proteins. In pulse-chase experiments it was apparent that p175 was a transient protein, as it was diminished during the chase, with a half-life of about 30 min. However, both p125 and p80 were also observed in short-pulsed lysates. Furthermore, during the chase, radiolabel was not found to accumulate into p125 or p80. Rather, these two proteins were stable with half-lives greater than 2 h. A fourth nonglycosylated protein, p37, increased during the chase. Processing of several glycoproteins was evident in these experiments. A glycoprotein of molecular weight 75 000 (gp75) diminished during the chase period, while glycoproteins gp62, gp48, and gp25 appeared or increased during the chase period. In contrast, the glycoprotein gp53 was a major protein in pulse-labeled cell lysates and remained constant throughout the chase period. In further experiments two stable forms of p80 differing in intramolecular disulphide bonding were observed. Key words: bovine viral diarrhea virus, proteins, relationships and processing, monoclonal antibodies.

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Schuster, M., E. Wasserbauer, G. Aversa, and A. Jungbauer. "Transmembrane-Sequence-Dependent Overexpression and Secretion of Glycoproteins in Saccharomyces cerevisiae." Protein Expression and Purification 21, no. 1 (February 2001): 1–7. http://dx.doi.org/10.1006/prep.2000.1337.

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31

NAIK, SANJAY, and SANJIT KUMAR. "APPLICATIONS OF PLANT LECTINS IN BIOTECHNOLOGY AND THERAPEUTICS." Journal of microbiology, biotechnology and food sciences 11, no. 4 (February 1, 2022): e4224. http://dx.doi.org/10.55251/jmbfs.4224.

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Lectins are carbohydrate-binding proteins broadly used in various therapeutic and biomedical applications. The variable affinity of lectins towards variety of carbohydrates has raised attention for the biologist to explore functional aspects of lectins. Lectins express specificity to simple carbohydrates for example mannose, lactose, sialic acid, complex glycan, and glycoproteins. Lectins are classified based on their sugar specificity and are used as a tool to study protein-carbohydrate interactions. Lectins are ubiquitous in nature and identified from all sources such as bacteria, fungi, algae, and animals. Plants are the most abundant source of lectins, and till now, more than three hundred lectins were characterized from plants. These are distributed to various parts of a plant according to their requirements and function. The physiological role of lectins in a plant is still not well understood. The overabundant presence of lectins in plant seeds and storage tissues indicated their role in plant development. Plant lectins shows a broad range of activities like antibacterial, antifungal, insecticidal, anticancerous, antileishmanial, antiviral, and anticoagulants. In this review, we aim to highlight the plant lectins classification and their application in various biological aspects.

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32

Katayama, Takane, Kiyotaka Fujita, and Kenji Yamamoto. "Novel bifidobacterial glycosidases acting on sugar chains of mucin glycoproteins." Journal of Bioscience and Bioengineering 99, no. 5 (May 2005): 457–65. http://dx.doi.org/10.1263/jbb.99.457.

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33

Lesman-Movshovich, Efrat, Batia Lerrer, and Nechama Gilboa-Garber. "Blocking ofPseudomonas aeruginosalectins by human milk glycans." Canadian Journal of Microbiology 49, no. 3 (March 1, 2003): 230–35. http://dx.doi.org/10.1139/w03-027.

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The opportunistic human pathogen Pseudomonas aeruginosa produces a D-galactophilic (PA-IL) lectin and another lectin (PA-IIL) that binds L-fucose > D-arabinose > D-mannose in close association with its host-attacking factors. These lectins contribute to the virulence of P. aeruginosa by their involvement in the production, adhesion, and pathogenic effects of its biofilm on host cells. Therefore, they are considered targets for anti-Pseudomonas therapy. The present study compares their blocking by human milk samples with that of the plant lectin Con A. It demonstrates that human milk inhibits the hemagglutinating activities of the three lectins, with PA-IIL much more strongly inhibited than PA-IL or Con A. Using these lectins, Western blots of the milk samples accord with the hemagglutination inhibition data and disclose the distribution of the human milk glycoproteins that inhibit each lectin. The data of this paper reveal the high efficiency of human milk components in blocking the P. aeruginosa lectins and the usefulness of these lectins for detecting milk glycoprotein saccharides, which may protect the infant against infections.Key words: Pseudomonas aeruginosa, lectins, human milk, glycoproteins, Western blotting.

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Paradkar, Vikram M., and Jonathan S. Dordick. "Purification of glycoproteins by selective transport using concanavalin-mediated reverse micellar extraction." Biotechnology Progress 7, no. 4 (July 1991): 330–34. http://dx.doi.org/10.1021/bp00010a007.

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Davis, Simon J., Michael J. Puklavec, David A. Ashford, Karl Harlos, E. Yvonne Jones, David I. Stuart, and Alan F. Williams. "Expression of soluble recombinant glycoproteins with predefined glycosylation: application to the crystallization of the T-cell glycoprotein CD2." "Protein Engineering, Design and Selection" 6, no. 2 (1993): 229–32. http://dx.doi.org/10.1093/protein/6.2.229.

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Anand, Sudha, Anand Anbarasu, and Rao Sethumadhavan. "Exploring the C–H…O Interactions in Glycoproteins." Applied Biochemistry and Biotechnology 159, no. 2 (January 21, 2009): 343–54. http://dx.doi.org/10.1007/s12010-008-8518-3.

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Buchholz, Christian J., Michael D. Mühlebach, and Klaus Cichutek. "Lentiviral vectors with measles virus glycoproteins – dream team for gene transfer?" Trends in Biotechnology 27, no. 5 (May 2009): 259–65. http://dx.doi.org/10.1016/j.tibtech.2009.02.002.

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Slade, Martin B., Kerry R. Emslie, and Keith L. Williams. "Expression of Recombinant Glycoproteins in the Simple EukaryoteDictyostelium discoideum." Biotechnology and Genetic Engineering Reviews 14, no. 1 (April 1997): 1–36. http://dx.doi.org/10.1080/02648725.1997.10647937.

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Vong, Kenward, Tomoya Yamamoto, and Katsunori Tanaka. "Artificial Glycoproteins as a Scaffold for Targeted Drug Therapy." Small 16, no. 27 (February 18, 2020): 1906890. http://dx.doi.org/10.1002/smll.201906890.

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40

Yang, Zhang, Shengjun Wang, Adnan Halim, Morten Alder Schulz, Morten Frodin, Shamim H. Rahman, Malene B. Vester-Christensen, et al. "Engineered CHO cells for production of diverse, homogeneous glycoproteins." Nature Biotechnology 33, no. 8 (July 20, 2015): 842–44. http://dx.doi.org/10.1038/nbt.3280.

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Takegawa, Kaoru, Kazunari Satoh, Nahrowi Ramli, Takayuki Jikibara, and Shojiro Iwahara. "Production and characterization of extracellular uronic acid-containing glycoproteins from Fusarium oxysporum." Journal of Fermentation and Bioengineering 83, no. 2 (January 1997): 197–200. http://dx.doi.org/10.1016/s0922-338x(97)83583-0.

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Rhee, Chang-Ho, and Heui-Dong Park. "Three Glycoproteins with Antimutagenic Activity Identified in Lactobacillus plantarum KLAB21." Applied and Environmental Microbiology 67, no. 8 (August 1, 2001): 3445–49. http://dx.doi.org/10.1128/aem.67.8.3445-3449.2001.

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ABSTRACT Antimutagenic substances were purified from a culture supernatant of Lactobacillus plantarum KLAB21 cells isolated from kimchi, a Korean traditional fermented vegetable, and their characteristics were investigated. The antimutagenic substances were separated into two fractions by DEAE-cellulose ion-exchange column chromatography, which were designated the R1 and R2 fractions. The R1 fraction was then divided into two fractions again by Sephadex G200 gel filtration chromatography, and the fractions were designated R1-1 and R1-2. All three fractions were further purified using a Sepharose CL-6B gel filtration column. All the purified fractions were successfully stained with fuchsin as well as Coomassie brilliant blue, suggesting that they are glycoproteins. The purified fractions were confirmed to possess antimutagenic activity againstN-methyl-N′-nitro-N-nitrosoguanidine on Salmonella enterica serovar Typhimurium TA100 cells. Their molecular masses were determined to be 16 (R1-1), 11 (R1-2), and 14 (R2) kDa on the Sepharose CL-6B column. Total sugar contents were 8.4% (R1-1), 7.3% (R1-2), and 9.4% (R2). The amino acid compositions of the fractions were different from each other; the major amino acids were glutamic acid (21.5%) and phenylalanine (17.1%) in the R1-1 fraction and glycine (41.3%) in the R1-2 fraction, but valine (31%) and phenylalanine (22.6%) were the major amino acids in the R2 fraction.

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Fisher, Adam C., Charles H. Haitjema, Cassandra Guarino, Eda Çelik, Christine E. Endicott, Craig A. Reading, Judith H. Merritt, A. Celeste Ptak, Sheng Zhang, and Matthew P. DeLisa. "Production of Secretory and Extracellular N-Linked Glycoproteins inEscherichia coli." Applied and Environmental Microbiology 77, no. 3 (December 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 on periplasmic proteins depending on their mode of inner membrane translocation (i.e., Sec, signal recognition particle [SRP], or twin-arginine translocation [Tat] export), indicating that the mode of protein export can influence N-glycosylation efficiency. We also established that engineered substrate proteins targeted to environments beyond the periplasm, such as the outer membrane, the membrane vesicles, and the extracellular medium, could serve as substrates for N-linked glycosylation. Taken together, our results demonstrate that theC. jejuniN-glycosylation machinery is compatible with distinct secretory mechanisms inE. coli, effectively expanding the N-linked glycome of recombinantE. coli. Moreover, this simple glycosylation tag strategy expands the glycoengineering toolbox and opens the door to bacterial synthesis of a wide array of recombinant glycoprotein conjugates.

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Jung, C., B. N. Grzybowski, S. Tong, L. Cheng, R. W. Compans, and J. M. LeDoux. "Lentiviral Vectors Pseudotyped with Envelope Glycoproteins Derived from Human Parainfluenza Virus Type 3." Biotechnology Progress 20, no. 6 (December 3, 2004): 1810–16. http://dx.doi.org/10.1021/bp049867h.

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Khan, Amjad Hayat, and Rahmah Noordin. "Strategies for humanizing glycosylation pathways and producing recombinant glycoproteins in microbial expression systems." Biotechnology Progress 35, no. 2 (December 6, 2018): e2752. http://dx.doi.org/10.1002/btpr.2752.

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Doig, Peter, William Paranchych, Parimi A. Sastry, and Randall T. Irvin. "Human buccal epithelial cell receptors of Pseudomonas aeruginosa: identification of glycoproteins with pilus binding activity." Canadian Journal of Microbiology 35, no. 12 (December 1, 1989): 1141–45. http://dx.doi.org/10.1139/m89-189.

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Adherence of Pseudomonas aeruginosa to a patient's epithelial surface is thought to be an important first step in the infection process. Pseudomonas aeruginosa is capable of attaching to epithelial cells via its pili, yet little is known about the epithelial receptors of this adhesin. Using nitrocellulose replicas of polyacrylamide gels of solubilized human buccal epithelial cells (BECs), glycoproteins (Mz: 82 000, and four bands between 40 000 and 50 000) that bound purified pili from P. aeruginosa strain K (PAK) were identified by immunoblotting with a pilus-specific monoclonal antibody that does not affect pilus binding to BECs (PK3B). All pilus-binding glycoproteins were surface localized, as determined by surface radioiodination of intact BECs. Binding of pili to all of the glycoproteins was inhibited by Fab fragments of monoclonal antibody PK99H, which inhibits PAK pili binding to BECs by binding to or near the binding domain of the pilus, but not by Fab fragments of monoclonal antibody PK41C, which binds to PAK pilin but does not inhibit pili binding to BECs, demonstrating that pilus binding to these glycoproteins is likely via the same region of the pilus that binds to intact BECs. Periodate oxidation of the blot eliminated pili binding to all glycoproteins, indicating that a carbohydrate moiety is an important determinant for pilus-binding activity. However, not all of the glycoproteins exhibited the same degree of sensitivity to periodate oxidation. Furthermore, monosaccharide inhibition of pilus binding to BECs implicated L-fucose and N-acetylneuraminic acid as receptor moieties.Key words: Pseudomonas aeruginosa, pili, receptor, adhesion.

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Wang, Zhao, Xiaojuan Zhang, Qing Lin, Jingjing Sun, Santanu Bhattachaya, Guosong Chen, and Ruilong Sheng. "Functional Glycopolypeptides: Synthesis and Biomedical Applications." Advances in Polymer Technology 2020 (June 2, 2020): 1–16. http://dx.doi.org/10.1155/2020/6052078.

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Employing natural-based renewable sugar and saccharide resources to construct functional biopolymer mimics is a promising research frontier for green chemistry and sustainable biotechnology. As the mimics/analogues of natural glycoproteins, synthetic glycopolypeptides attracted great attention in the field of biomaterials and nanobiotechnology. This review describes the synthetic strategies and methods of glycopolypeptides and their analogues, the functional self-assemblies of the synthesized glycopolypeptides, and their biological applications such as biomolecular recognition, drug/gene delivery, and cell adhesion and targeting, as well as cell culture and tissue engineering. Future outlook of the synthetic glycopolypeptides was also discussed.

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Orellana, Adelina, David Mottershead, Inge van der Linden, Kari Keinänen, and Christian Oker-Blom. "Mimicking rubella virus particles by using recombinant envelope glycoproteins and liposomes." Journal of Biotechnology 75, no. 2-3 (October 1999): 209–19. http://dx.doi.org/10.1016/s0168-1656(99)00162-5.

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Mikami, Satoshi, Tominari Kobayashi, Shigeyuki Yokoyama, and Hiroaki Imataka. "A hybridoma-based in vitro translation system that efficiently synthesizes glycoproteins." Journal of Biotechnology 127, no. 1 (December 2006): 65–78. http://dx.doi.org/10.1016/j.jbiotec.2006.06.018.

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James, David C. "Analysis of recombinat glycoproteins by mass spectrometry." Cytotechnology 22, no. 1-3 (1996): 17–24. http://dx.doi.org/10.1007/bf00353920.

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