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  1. AU="Klontz, Erik H"
  2. AU=Lu Chen Chen
  3. AU="Shabsovich, David"
  4. AU="Foraker, Randi E"
  5. AU="Kolonko, Aureliusz"
  6. AU=Falagas M E
  7. AU="Dunstan, Melanie L"
  8. AU=Kacar Mark AU=Kacar Mark
  9. AU="Schaup, Rebecca Michaela"
  10. AU="Ye, Chaofu"
  11. AU="Tekin, Nur"
  12. AU="Martens, Dirk E"
  13. AU=Teos Leyla Y.
  14. AU="Sánchez-Garcia, Joaquín"
  15. AU="Schaller, Benoit"
  16. AU="Hernandez, A"
  17. AU="Nguyen, Thien H"
  18. AU="Park, Jung Wan"
  19. AU="Mahajan, Aman"
  20. AU="Hao, Yanling"
  21. AU="Eing, Lorenz"
  22. AU="Geoffroy, Pierre A"
  23. AU="Chapuis, J"
  24. AU="Berta, László"
  25. AU="Barzilay, Regina"
  26. AU="Schmidt, Michael Rahbek"
  27. AU=Tack J
  28. AU="Oh, Hye Min"
  29. AU=Gaffen Sarah L AU=Gaffen Sarah L
  30. AU="Schmitt, Christine"
  31. AU="McKay, Jackie"
  32. AU="Bellissimo, Catherine A"
  33. AU="Desai, Urja"
  34. AU="Chini, Maria Giovanna"
  35. AU="Xiao, Difei"
  36. AU="Ryan, Chris"
  37. AU="Omar Bazighifan"
  38. AU="Corominas Galbany, Jordi"
  39. AU=Fox Norma E
  40. AU="Hamilton, Shelia M"
  41. AU="Nichols, J Wylie"
  42. AU="Pesce R."
  43. AU="Gambitta, P"
  44. AU="Imran, Aqeel"
  45. AU="Sharma, Yashoda"
  46. AU="Kosai, Jordyn"
  47. AU="Aroca Ferri, María"
  48. AU="Laba, Stephanie"
  49. AU="Kim, Ye-Sel"

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Treffer 1 - 10 von insgesamt 20

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  1. Artikel ; Online: Chop-Chop: The Future of Bacterial Enzymes in Transfusion Medicine.

    Klontz, Erik H

    Transfusion medicine reviews

    2022  Band 36, Heft 4, Seite(n) 246–251

    Abstract: The discovery of bacterial enzymes with specificity for IgG antibodies has led to breakthroughs in several autoantibody-mediated diseases. Two such enzymes, IdeS and EndoS, degrade IgG by different mechanisms, and have separately shown promise in ... ...

    Abstract The discovery of bacterial enzymes with specificity for IgG antibodies has led to breakthroughs in several autoantibody-mediated diseases. Two such enzymes, IdeS and EndoS, degrade IgG by different mechanisms, and have separately shown promise in numerous animal models of autoimmune diseases. Recently, imlifidase (the international nonproprietary name for IdeS) has advanced to clinical trials, where it has performed remarkably well in desensitizing patients to enable kidney transplantation, and in anti-glomerular basement membrane disease. Conversely, it performed poorly in thrombotic thrombocytopenic purpura. This review summarizes the development of antibody-degrading enzymes, with a discussion of key clinical studies involving imlifidase. The future of the field is also discussed, including the use of these enzymes in other diseases, and the potential for re-dosing.
    Mesh-Begriff(e) Animals ; Humans ; Transfusion Medicine ; Bacterial Proteins/therapeutic use ; Anti-Glomerular Basement Membrane Disease/drug therapy ; Immunoglobulin G ; Autoantibodies ; Immunosuppressive Agents/therapeutic use
    Chemische Substanzen Bacterial Proteins ; Immunoglobulin G ; Autoantibodies ; Immunosuppressive Agents
    Sprache Englisch
    Erscheinungsdatum 2022-08-28
    Erscheinungsland United States
    Dokumenttyp Review ; Journal Article
    ZDB-ID 639107-2
    ISSN 1532-9496 ; 0887-7963
    ISSN (online) 1532-9496
    ISSN 0887-7963
    DOI 10.1016/j.tmrv.2022.05.003
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  2. Artikel ; Online: Case 4-2024: A 39-Year-Old Man with Fever and Headache after International Travel.

    Ryan, Edward T / Succi, Marc D / Paras, Molly L / Klontz, Erik H

    The New England journal of medicine

    2024  Band 390, Heft 6, Seite(n) 549–556

    Mesh-Begriff(e) Adult ; Humans ; Male ; Fever/etiology ; Headache/etiology ; Travel ; Internationality ; Travel-Related Illness
    Sprache Englisch
    Erscheinungsdatum 2024-02-07
    Erscheinungsland United States
    Dokumenttyp Case Reports ; Journal Article
    ZDB-ID 207154-x
    ISSN 1533-4406 ; 0028-4793
    ISSN (online) 1533-4406
    ISSN 0028-4793
    DOI 10.1056/NEJMcpc2309382
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  3. Artikel ; Online: Cerebrospinal fluid metagenomics has greatest added value as a test for Powassan virus among patients in New England with suspected central nervous system infection.

    Klontz, Erik H / Solomon, Isaac H / Turbett, Sarah E / Lemieux, Jacob E / Branda, John A

    Diagnostic microbiology and infectious disease

    2024  Band 108, Heft 4, Seite(n) 116169

    Abstract: Cerebrospinal fluid (CSF) metagenomic next generation sequencing (mNGS) can detect diverse pathogens in patients with central nervous system infection. Due to its high cost and unclear clinical utility, it is typically reserved for patients with ... ...

    Abstract Cerebrospinal fluid (CSF) metagenomic next generation sequencing (mNGS) can detect diverse pathogens in patients with central nervous system infection. Due to its high cost and unclear clinical utility, it is typically reserved for patients with unrevealing routine workups. A multi-center retrospective analysis of real-world CSF mNGS was performed involving orders between 2017 and 2022 at a large New England healthcare system. CSF mNGS was performed 64 times with 17 positive results (27 %). In 11/17 positive samples (65 %), the infectious agent had not been previously detected using routine methods. Arboviruses (n = 8) were the most frequently detected agents, particularly Powassan virus (n = 6). Results changed therapy in 3/64 cases (5 %). Positive results were associated with immunodeficiency (p = 0.06), especially anti-B-cell therapy (p = 0.02), and earlier sample collection (p = 0.06). The association with compromised humoral immunity was stronger in the arbovirus and Powassan virus subgroups (p = 0.001), whose constituents were older than the overall cohort and had higher mortality rates.
    Mesh-Begriff(e) Humans ; Central Nervous System Infections ; Encephalitis Viruses, Tick-Borne ; High-Throughput Nucleotide Sequencing ; Metagenomics/methods ; New England ; Retrospective Studies ; Sensitivity and Specificity
    Sprache Englisch
    Erscheinungsdatum 2024-01-04
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Multicenter Study
    ZDB-ID 604920-5
    ISSN 1879-0070 ; 0732-8893
    ISSN (online) 1879-0070
    ISSN 0732-8893
    DOI 10.1016/j.diagmicrobio.2023.116169
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  4. Artikel: Babesia microti

    Holbrook, Nolan R / Klontz, Erik H / Adams, Gordon C / Schnittman, Samuel R / Issa, Nicolas C / Bond, Sheila A / Branda, John A / Lemieux, Jacob E

    Open forum infectious diseases

    2023  Band 10, Heft 3, Seite(n) ofad097

    Abstract: ... We ... ...

    Abstract We report
    Sprache Englisch
    Erscheinungsdatum 2023-02-23
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 2757767-3
    ISSN 2328-8957
    ISSN 2328-8957
    DOI 10.1093/ofid/ofad097
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  5. Artikel ; Online: Getting oriented with antibodies.

    Klontz, Erik H / Sundberg, Eric J

    The Biochemical journal

    2017  Band 474, Heft 4, Seite(n) 517–519

    Abstract: Neisseria meningitidis is a Gram-negative bacterium capable of causing deadly invasive disease. Two recently developed vaccines against N. meningitidis serogroup B include recombinant factor H binding protein (fHbp), a surface protein that meningococci ... ...

    Abstract Neisseria meningitidis is a Gram-negative bacterium capable of causing deadly invasive disease. Two recently developed vaccines against N. meningitidis serogroup B include recombinant factor H binding protein (fHbp), a surface protein that meningococci use to evade the host immune system. Many anti-fHbp monoclonal antibodies (mAbs) produced against fHbp fail to trigger complement-mediated bacteriolysis when used alone in vitro, but are highly synergistic and bactericidal when used in combination. This opened the door to defining the structural basis by which mAbs activate complement synergistically when binding to different epitopes on the same antigen, a story that is told by Malito et al. in a recent issue of the Biochemical Journal. Using two separate crystal structures of fHbp bound to Fabs from synergistic mAbs, they were able to model the structure of both full length antibodies bound simultaneously to fHbp. This revealed that the bound antibodies orient their Fc domains 115-130 Å apart, a distance that is compatible with multivalent C1q binding. The need for a precise orientation of Fc domains in order to efficiently activate effector functions is an emerging theme across multiple fields, and its implications could have broad impacts on vaccinology and immunotherapy.
    Mesh-Begriff(e) Antibodies, Bacterial/biosynthesis ; Antibodies, Bacterial/chemistry ; Antibodies, Bacterial/pharmacology ; Antibodies, Monoclonal/biosynthesis ; Antibodies, Monoclonal/chemistry ; Antibodies, Monoclonal/pharmacology ; Antigens, Bacterial/chemistry ; Antigens, Bacterial/immunology ; Bacterial Proteins/antagonists & inhibitors ; Bacterial Proteins/chemistry ; Bacterial Proteins/immunology ; Binding Sites, Antibody ; Complement C1q/chemistry ; Complement C1q/metabolism ; Crystallography, X-Ray ; Drug Synergism ; Drug Therapy, Combination ; Epitopes/chemistry ; Epitopes/immunology ; Immunoglobulin Fab Fragments/chemistry ; Immunoglobulin Fab Fragments/immunology ; Immunoglobulin Fc Fragments/chemistry ; Immunoglobulin Fc Fragments/immunology ; Neisseria meningitidis/chemistry ; Neisseria meningitidis/drug effects ; Neisseria meningitidis/immunology ; Protein Binding
    Chemische Substanzen Antibodies, Bacterial ; Antibodies, Monoclonal ; Antigens, Bacterial ; Bacterial Proteins ; Epitopes ; Immunoglobulin Fab Fragments ; Immunoglobulin Fc Fragments ; factor H-binding protein, Neisseria meningitidis ; Complement C1q (80295-33-6)
    Sprache Englisch
    Erscheinungsdatum 2017-02-15
    Erscheinungsland England
    Dokumenttyp Journal Article
    ZDB-ID 2969-5
    ISSN 1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
    ISSN (online) 1470-8728
    ISSN 0006-2936 ; 0306-3275 ; 0264-6021
    DOI 10.1042/BCJ20160996
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  6. Artikel ; Online: Sculpting therapeutic monoclonal antibody N-glycans using endoglycosidases.

    Trastoy, Beatriz / Du, Jonathan J / García-Alija, Mikel / Li, Chao / Klontz, Erik H / Wang, Lai-Xi / Sundberg, Eric J / Guerin, Marcelo E

    Current opinion in structural biology

    2022  Band 72, Seite(n) 248–259

    Abstract: Immunoglobulin G (IgG) monoclonal antibodies are a prominent and expanding class of therapeutics used for the treatment of diverse human disorders. The chemical composition of the N-glycan on the fragment crystallizable (Fc) region determines the ... ...

    Abstract Immunoglobulin G (IgG) monoclonal antibodies are a prominent and expanding class of therapeutics used for the treatment of diverse human disorders. The chemical composition of the N-glycan on the fragment crystallizable (Fc) region determines the effector functions through interaction with the Fc gamma receptors and complement proteins. The chemoenzymatic synthesis using endo-β-N-acetylglucosaminidases (ENGases) emerged as a strategy to obtain antibodies with customized glycoforms that modulate their therapeutic activity. We discuss the molecular mechanism by which ENGases recognize different N-glycans and protein substrates, especially those that are specific for IgG antibodies, in order to rationalize the glycoengineering of immunotherapeutic antibodies, which increase the impact on the treatment of myriad diseases.
    Mesh-Begriff(e) Antibodies, Monoclonal/chemistry ; Glycoside Hydrolases/metabolism ; Glycosylation ; Humans ; Immunoglobulin Fc Fragments/chemistry ; Immunoglobulin Fc Fragments/metabolism ; Immunoglobulin G/chemistry ; Immunoglobulin G/metabolism ; Polysaccharides/metabolism
    Chemische Substanzen Antibodies, Monoclonal ; Immunoglobulin Fc Fragments ; Immunoglobulin G ; Polysaccharides ; Glycoside Hydrolases (EC 3.2.1.-)
    Sprache Englisch
    Erscheinungsdatum 2022-01-05
    Erscheinungsland England
    Dokumenttyp 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.2021.11.016
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  7. Artikel ; Online: Mass Spectrometry-Based Methods to Determine the Substrate Specificities and Kinetics of N-Linked Glycan Hydrolysis by Endo-β-N-Acetylglucosaminidases.

    Du, Jonathan J / Sastre, Diego / Trastoy, Beatriz / Roberts, Blaine / Deredge, Daniel / Klontz, Erik H / Flowers, Maria W / Sultana, Nazneen / Guerin, Marcelo E / Sundberg, Eric J

    Methods in molecular biology (Clifton, N.J.)

    2023  Band 2674, Seite(n) 147–167

    Abstract: Glycosylation is a common posttranslational modification of proteins and refers to the covalent addition of glycans, chains of polysaccharides, onto proteins producing glycoproteins. The glycans influence the structure, function, and stability of ... ...

    Abstract Glycosylation is a common posttranslational modification of proteins and refers to the covalent addition of glycans, chains of polysaccharides, onto proteins producing glycoproteins. The glycans influence the structure, function, and stability of proteins. They also play an integral role in the immune system, and aberrantly glycosylated proteins have wide ranging effects, including leading to diseases such as autoimmune conditions and cancer. Carbohydrate-active enzymes (CAZymes) are produced in bacteria, fungi, and humans and are enzymes which modify glycans via the addition or subtraction of individual or multiple saccharides from glycans. One of the hurdles in studying these enzymes is determining the types of substrates each enzyme is specific for and the kinetics of enzymatic activity. In this chapter, we discuss methods which are currently used to study the substrate specificity and kinetics of CAZymes and introduce a novel mass spectrometry-based technique which enables the specificity and kinetics of CAZymes to be determined accurately and efficiently.
    Mesh-Begriff(e) Humans ; Substrate Specificity ; Acetylglucosaminidase/metabolism ; Hydrolysis ; Kinetics ; Mass Spectrometry/methods ; Polysaccharides/chemistry
    Chemische Substanzen Acetylglucosaminidase (EC 3.2.1.52) ; Polysaccharides
    Sprache Englisch
    Erscheinungsdatum 2023-05-30
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-3243-7_10
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  8. Artikel ; Online: Insights into substrate recognition and specificity for IgG by Endoglycosidase S2.

    Aytenfisu, Asaminew H / Deredge, Daniel / Klontz, Erik H / Du, Jonathan / Sundberg, Eric J / MacKerell, Alexander D

    PLoS computational biology

    2021  Band 17, Heft 7, Seite(n) e1009103

    Abstract: Antibodies bind foreign antigens with high affinity and specificity leading to their neutralization and/or clearance by the immune system. The conserved N-glycan on IgG has significant impact on antibody effector function, with the endoglycosidases of ... ...

    Abstract Antibodies bind foreign antigens with high affinity and specificity leading to their neutralization and/or clearance by the immune system. The conserved N-glycan on IgG has significant impact on antibody effector function, with the endoglycosidases of Streptococcus pyogenes deglycosylating the IgG to evade the immune system, a process catalyzed by the endoglycosidase EndoS2. Studies have shown that two of the four domains of EndoS2, the carbohydrate binding module (CBM) and the glycoside hydrolase (GH) domain are critical for catalytic activity. To yield structural insights into contributions of the CBM and the GH domains as well as the overall flexibility of EndoS2 to the proteins' catalytic activity, models of EndoS2-Fc complexes were generated through enhanced-sampling molecular-dynamics (MD) simulations and site-identification by ligand competitive saturation (SILCS) docking followed by reconstruction and multi-microsecond MD simulations. Modeling results predict that EndoS2 initially interacts with the IgG through its CBM followed by interactions with the GH yielding catalytically competent states. These may involve the CBM and GH of EndoS2 simultaneously interacting with either the same Fc CH2/CH3 domain or individually with the two Fc CH2/CH3 domains, with EndoS2 predicted to assume closed conformations in the former case and open conformations in the latter. Apo EndoS2 is predicted to sample both the open and closed states, suggesting that either complex can directly form following initial IgG-EndoS2 encounter. Interactions of the CBM and GH domains with the IgG are predicted to occur through both its glycan and protein regions. Simulations also predict that the Fc glycan can directly transfer from the CBM to the GH, facilitating formation of catalytically competent complexes and how the 734 to 751 loop on the CBM can facilitate extraction of the glycan away from the Fc CH2/CH3 domain. The predicted models are compared and consistent with Hydrogen/Deuterium Exchange data. In addition, the complex models are consistent with the high specificity of EndoS2 for the glycans on IgG supporting the validity of the predicted models.
    Mesh-Begriff(e) Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Computational Biology ; Deuterium Exchange Measurement ; Glycoside Hydrolases/chemistry ; Glycoside Hydrolases/metabolism ; Humans ; Immunoglobulin Fc Fragments/chemistry ; Immunoglobulin Fc Fragments/metabolism ; Immunoglobulin G/chemistry ; Immunoglobulin G/metabolism ; Molecular Dynamics Simulation ; Polysaccharides/chemistry ; Polysaccharides/metabolism ; Protein Conformation ; Streptococcus pyogenes/enzymology ; Substrate Specificity
    Chemische Substanzen Bacterial Proteins ; Immunoglobulin Fc Fragments ; Immunoglobulin G ; Polysaccharides ; Glycoside Hydrolases (EC 3.2.1.-)
    Sprache Englisch
    Erscheinungsdatum 2021-07-26
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2193340-6
    ISSN 1553-7358 ; 1553-734X
    ISSN (online) 1553-7358
    ISSN 1553-734X
    DOI 10.1371/journal.pcbi.1009103
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  9. Artikel ; Online: Structural insights into the mechanisms and specificities of IgG-active endoglycosidases.

    Du, Jonathan J / Klontz, Erik H / Guerin, Marcelo E / Trastoy, Beatriz / Sundberg, Eric J

    Glycobiology

    2019  Band 30, Heft 4, Seite(n) 268–279

    Abstract: The conserved N-glycan on Asn297 of immunoglobulin G (IgG) has significant impacts on antibody effector functions, and is a frequent target for antibody engineering. Chemoenzymatic synthesis has emerged as a strategy for producing antibodies with ... ...

    Abstract The conserved N-glycan on Asn297 of immunoglobulin G (IgG) has significant impacts on antibody effector functions, and is a frequent target for antibody engineering. Chemoenzymatic synthesis has emerged as a strategy for producing antibodies with homogenous glycosylation and improved effector functions. Central to this strategy is the use of enzymes with activity on the Asn297 glycan. EndoS and EndoS2, produced by Streptococcus pyogenes, are endoglycosidases with remarkable specificity for Asn297 glycosylation, making them ideal tools for chemoenzymatic synthesis. Although both enzymes are specific for IgG, EndoS2 recognizes a wider range of glycans than EndoS. Recent progress has been made in understanding the structural basis for their activities on antibodies. In this review, we examine the molecular mechanism of glycosidic bond cleavage by these enzymes and how specific point mutations convert them into glycosynthases. We also discuss the structural basis for differences in the glycan repertoire that IgG-active endoglycosidases recognize, which focuses on the structure of the loops within the glycoside hydrolase (GH) domain. Finally, we discuss the important contributions of carbohydrate binding modules (CBMs) to endoglycosidase activity, and how CBMs work in concert with GH domains to produce optimal activity on IgG.
    Mesh-Begriff(e) Animals ; Glycoside Hydrolases/metabolism ; Glycosylation ; Humans ; Immunoglobulin G/chemistry ; Immunoglobulin G/metabolism ; Models, Molecular ; Molecular Structure ; Polysaccharides/chemistry ; Polysaccharides/metabolism ; Streptococcus pyogenes/enzymology
    Chemische Substanzen Immunoglobulin G ; Polysaccharides ; Glycoside Hydrolases (EC 3.2.1.-)
    Sprache Englisch
    Erscheinungsdatum 2019-06-07
    Erscheinungsland England
    Dokumenttyp Journal Article ; Review
    ZDB-ID 1067689-2
    ISSN 1460-2423 ; 0959-6658
    ISSN (online) 1460-2423
    ISSN 0959-6658
    DOI 10.1093/glycob/cwz042
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  10. Artikel ; Online: Mechanism of antibody-specific deglycosylation and immune evasion by Streptococcal IgG-specific endoglycosidases.

    Trastoy, Beatriz / Du, Jonathan J / Cifuente, Javier O / Rudolph, Lorena / García-Alija, Mikel / Klontz, Erik H / Deredge, Daniel / Sultana, Nazneen / Huynh, Chau G / Flowers, Maria W / Li, Chao / Sastre, Diego E / Wang, Lai-Xi / Corzana, Francisco / Mallagaray, Alvaro / Sundberg, Eric J / Guerin, Marcelo E

    Nature communications

    2023  Band 14, Heft 1, Seite(n) 1705

    Abstract: Bacterial pathogens have evolved intricate mechanisms to evade the human immune system, including the production of immunomodulatory enzymes. Streptococcus pyogenes serotypes secrete two multi-modular endo-β-N-acetylglucosaminidases, EndoS and EndoS2, ... ...

    Abstract Bacterial pathogens have evolved intricate mechanisms to evade the human immune system, including the production of immunomodulatory enzymes. Streptococcus pyogenes serotypes secrete two multi-modular endo-β-N-acetylglucosaminidases, EndoS and EndoS2, that specifically deglycosylate the conserved N-glycan at Asn297 on IgG Fc, disabling antibody-mediated effector functions. Amongst thousands of known carbohydrate-active enzymes, EndoS and EndoS2 represent just a handful of enzymes that are specific to the protein portion of the glycoprotein substrate, not just the glycan component. Here, we present the cryoEM structure of EndoS in complex with the IgG1 Fc fragment. In combination with small-angle X-ray scattering, alanine scanning mutagenesis, hydrolytic activity measurements, enzyme kinetics, nuclear magnetic resonance and molecular dynamics analyses, we establish the mechanisms of recognition and specific deglycosylation of IgG antibodies by EndoS and EndoS2. Our results provide a rational basis from which to engineer novel enzymes with antibody and glycan selectivity for clinical and biotechnological applications.
    Mesh-Begriff(e) Humans ; Glycoside Hydrolases/metabolism ; Immune Evasion ; Streptococcus pyogenes ; Immunoglobulin G ; Polysaccharides/metabolism
    Chemische Substanzen Glycoside Hydrolases (EC 3.2.1.-) ; Immunoglobulin G ; Polysaccharides
    Sprache Englisch
    Erscheinungsdatum 2023-03-27
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-37215-3
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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