CoChat
Sign Up
Cited by 8

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

Mini Review: Structure and Function of Nematode Phosphorylcholine-Containing Glycoconjugates

Buitrago, Geraldine, Duncombe-Moore, Josephine, Harnett, Margaret M., Harnett, William·2021·Frontiers in Tropical Diseases
DOI 10.3389/fitd.2021.769000
Open this paper in CoChat — free account

Abstract

An unusual aspect of the biology of nematodes is the covalent attachment of phosphorylcholine (PC) to carbohydrate in glycoconjugates. Investigation of the structure of these molecules by ever-increasingly sophisticated analytical procedures has revealed that PC is generally in phosphodiester linkage with C6 of N-acetylglucosamine (GlcNAc) in both N-type glycans and glycosphingolipids. Up to five PC groups have been detected in the former, being located on both antenna and core GlcNAc. The PC donor for transfer to carbohydrate appears to be phosphatidylcholine but the enzyme responsible for transfer remains to be identified. Work primarily involving the PC-containing Acanthocheilonema viteae secreted product ES-62, has shown that the PC attached to nematode N-glycans possesses a range of immunomodulatory properties, subverting for example, pro-inflammatory signalling in various immune system cell-types including lymphocytes, mast cells, dendritic cells and macrophages. This has led to the generation of PC-based ES-62 small molecule analogues (SMAs), which mirror the parent molecule in preventing the initiation or progression of disease in mouse models of a number of human conditions associated with aberrant inflammatory responses. These include rheumatoid arthritis, systemic lupus erythematosus and lung and skin allergy such that the SMAs are considered to have widespread therapeutic potential.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.3389/fitd.2021.769000

Cites

3 of 3 references verified0 citation errors · 0 not checkable

Statistics

Figures

Image 1
CC-BY · From the PDF
Image 2
CC-BY · From the PDF
FIGURE 3 ES-62/phosphorylcholine (PC) desensitises immune system cell signalling in vitro . (A) The B cell antigen receptor (BCR) signals via ITAM-containing Ig a / b accessory molecules to recruit proliferative signalling pathways like the ERK MAPK cascade in a tyrosine kinase-dependent manner. PC/ES-62 desensitises the BCR both by recruiting SHP-1 to dephosphorylate Ig b and uncouple downstream signalling and by inducing DUSP2 dephosphorylation of the TEY activation motif of ERK1/2. (B) Fc ϵ RI-mediated degranulation requires calcium and PKC a signalling whilst, at least in some mast cell subsets, cytokine secretion also requires crosstalk with MyD88 signalling and all of these elements are targeted by PC/ES-62. (C) TLR4 homodimer and TLR1/2 heterodimer located at the cell surface on dendritic cells and macrophages signal through the adaptor proteins TIRAP and MyD88 in response to LPS and bacterial lipopeptide (e.g., PAM3CSK4) respectively. TLR9, which responds to unmethylated cytosine-phosphate-guanine (CpG) DNA, also signals through MyD88. MyD88 stimulates NFk B regulated proin fl ammatory cytokine production. ES-62 and PC-conjugated proteins subvert TLR4-MyD88 signalling to reduce proin fl ammatory cytokine secretion in response to TLR1/2, TLR4 and TLR9 ligation. Small molecule analogues 11a and 12b interact directly with MyD88 thereby similarly inhibiting cytokine production. TLR3 signalling, which is MyD88independent, is not affected by these anti-in fl ammatory agents. ES-62 is internalised by macrophages and may also directly interact with MyD88 via its PC moieties.
FIGURE 3 ES-62/phosphorylcholine (PC) desensitises immune system cell signalling in vitro . (A) The B cell antigen receptor (BCR) signals via ITAM-containing Ig a / b accessory molecules to recruit proliferative signalling pathways like the ERK MAPK cascade in a tyrosine kinase-dependent manner. PC/ES-62 desensitises the BCR both by recruiting SHP-1 to dephosphorylate Ig b and uncouple downstream signalling and by inducing DUSP2 dephosphorylation of the TEY activation motif of ERK1/2. (B) Fc ϵ RI-mediated degranulation requires calcium and PKC a signalling whilst, at least in some mast cell subsets, cytokine secretion also requires crosstalk with MyD88 signalling and all of these elements are targeted by PC/ES-62. (C) TLR4 homodimer and TLR1/2 heterodimer located at the cell surface on dendritic cells and macrophages signal through the adaptor proteins TIRAP and MyD88 in response to LPS and bacterial lipopeptide (e.g., PAM3CSK4) respectively. TLR9, which responds to unmethylated cytosine-phosphate-guanine (CpG) DNA, also signals through MyD88. MyD88 stimulates NFk B regulated proin fl ammatory cytokine production. ES-62 and PC-conjugated proteins subvert TLR4-MyD88 signalling to reduce proin fl ammatory cytokine secretion in response to TLR1/2, TLR4 and TLR9 ligation. Small molecule analogues 11a and 12b interact directly with MyD88 thereby similarly inhibiting cytokine production. TLR3 signalling, which is MyD88independent, is not affected by these anti-in fl ammatory agents. ES-62 is internalised by macrophages and may also directly interact with MyD88 via its PC moieties.CC-BY · From the PDF
FIGURE 4 ES-62/PC-mechanism of action in collagen-induced arthritis and ovalbumin-induced airway hyperresponsiveness. In collagen induced arthritis (CIA), during the initiation phase, gd T cells and T helper (Th)17 cells secrete interleukin (IL)-17 and IL-22 causing joint pathology. By contrast, during established disease IL22 acts to limit pathology, indicating that this cytokine plays dual pathogenic and protective roles in CIA. Treatment with ES-62 or small molecule analogue (SMA) 11a inhibits IL-17 production and ES-62 promotes protective IL-22 production as well as restoring regulatory B cell (Breg) responses to counter pathogenic effector B cell (Beff) responses including collagen-speci fi c IgG2a production, thereby substantially reducing arthritis. In ovalbumin-induced airway hyperresponsiveness (AHR), in fl ammatory immune system cells such as eosinophils and neutrophils in fi ltrate the lungs, generating IL-4 production, and a Th2 anti-in fl ammatory immunological phenotype is evident in immune cells in draining lymph nodes as the cells secrete IL-5 and IL-13 upon re-stimulation ex vivo . ES-62 and SMA administration reduce the in fi ltration of in fl ammatory immune cells and the former has also been shown to inhibit the ex vivo production of IL-5 and IL-13. Moreover, ES-62-activity in this model has been found to be dependent on IFNg and in addition, similar to CIA, the helminth product increases IL-10-producing Bregs.
FIGURE 4 ES-62/PC-mechanism of action in collagen-induced arthritis and ovalbumin-induced airway hyperresponsiveness. In collagen induced arthritis (CIA), during the initiation phase, gd T cells and T helper (Th)17 cells secrete interleukin (IL)-17 and IL-22 causing joint pathology. By contrast, during established disease IL22 acts to limit pathology, indicating that this cytokine plays dual pathogenic and protective roles in CIA. Treatment with ES-62 or small molecule analogue (SMA) 11a inhibits IL-17 production and ES-62 promotes protective IL-22 production as well as restoring regulatory B cell (Breg) responses to counter pathogenic effector B cell (Beff) responses including collagen-speci fi c IgG2a production, thereby substantially reducing arthritis. In ovalbumin-induced airway hyperresponsiveness (AHR), in fl ammatory immune system cells such as eosinophils and neutrophils in fi ltrate the lungs, generating IL-4 production, and a Th2 anti-in fl ammatory immunological phenotype is evident in immune cells in draining lymph nodes as the cells secrete IL-5 and IL-13 upon re-stimulation ex vivo . ES-62 and SMA administration reduce the in fi ltration of in fl ammatory immune cells and the former has also been shown to inhibit the ex vivo production of IL-5 and IL-13. Moreover, ES-62-activity in this model has been found to be dependent on IFNg and in addition, similar to CIA, the helminth product increases IL-10-producing Bregs.CC-BY · From the PDF

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 3 references

Research works printed but not linked: 112

  1. Brooker, 2004, Human Hookworm Infection in the 21st Century, Adv Parasitol, 58, 197, 10.1016/S0065-308X(04)58004-1 · DOI
  2. Recker, 2004, Transient Cross-Reactive Immune Responses can Orchestrate Antigenic Variation in Malaria, Nature, 429, 10.1038/nature02486 · DOI
  3. Leow, 2015, Structure-Function Analysis of Apical Membrane-Associated Molecules of the Tegument of Schistosome Parasites of Humans: Prospects for Identification of Novel Targets for Parasite Control, Br J Pharmacol, 172, 10.1111/bph.12898 · DOI
  4. Péry, 1974, Phosphorylcholine-Bearing Components in Homogenates of Nematodes, Eur J Immunol, 4, 10.1002/eji.1830040914 · DOI
  5. Forsyth, 1984, Onchocerca Gibsoni: Increase of Circulating Egg Antigen With Chemotherapy in Bovines, Exp Parasitol, 58, 41, 10.1016/0014-4894(84)90019-5 · DOI
  6. Forsyth, 1985, A Monoclonal Antibody-Based Immunoradiometric Assay for Detection of Circulating Antigen in Bancroftian Filariasis, J Immunol, 134, 1172, 10.4049/jimmunol.134.2.1172 · DOI
  7. Lal, 1987, Circulating Parasite Antigen(s) in Lymphatic Filariasis: Use of Monoclonal Antibodies to Phosphocholine for Immunodiagnosis, J Immunol, 138, 3454, 10.4049/jimmunol.138.10.3454 · DOI
  8. Maizels, 1987, Phosphorylcholine-Bearing Antigens in Filarial Nematode Parasites: Analysis of Somatic Extracts, in-Vitro Secretions and Infection Sera From Brugia Malayi and B. Pahangi, Parasite Immunol, 9, 49, 10.1111/j.1365-3024.1987.tb00488.x · DOI
  9. Weiss, 1986, Detection of Serum Antibodies and Circulating Antigens in a Chimpanzee Experimentally Infected With Onchocerca Volvulus, Trans R Soc Trop Med Hyg, 80, 10.1016/0035-9203(86)90150-1 · DOI
  10. Wenger, 1988, Identification of Phosphorylcholine Epitope-Containing Antigens in Brugia Malayi and Relation of Serum Epitope Levels to Infection Status of Jirds With Brugian Filariasis, Am J Trop Med Hyg, 38, 10.4269/ajtmh.1988.38.133 · DOI
  11. Harnett, 1989, Origin, Kinetics of Circulation and Fate In Vivo of the Major Excretory–Secretory Product of Acanthocheilonema Viteae, Parasitology, 99, 10.1017/S0031182000058686 · DOI
  12. Haslam, 1999, Structural Studies of N-Glycans of Filarial Parasites. Conservation of Phosphorylcholine-Substituted Glycans Among Species and Discovery of Novel Chito-Oligomers, J Biol Chem, 274, 10.1074/jbc.274.30.20953 · DOI
  13. Wuhrer, 2000, Phosphocholine-Containing, Zwitterionic Glycosphingolipids of Adult Onchocerca Volvulus as Highly Conserved Antigenic Structures of Parasitic Nematodes, Biochem J, 10.1042/bj3480417 · DOI
  14. Deehan, 2002, Immunomodulatory Properties of Ascaris Suum Glycosphingolipids – Phosphorylcholine and Non-Phosphorylcholine-Dependent Effects, Parasite Immunol, 24, 10.1046/j.1365-3024.2002.00489.x · DOI
  15. Pöltl, 2007, N-Glycans of the Porcine Nematode Parasite Ascaris Suum Are Modified With Phosphorylcholine and Core Fucose Residues, FEBS J, 274, 10.1111/j.1742-4658.2006.05615.x · DOI
  16. Hewitson, 2008, The Secretome of the Filarial Parasite, Brugia Malayi: Proteomic Profile of Adult Excretory-Secretory Products, Mol Biochem Parasitol, 160, 8, 10.1016/j.molbiopara.2008.02.007 · DOI
  17. Martini, 2019, Highly Modified and Immunoactive N-Glycans of the Canine Heartworm, Nat Commun, 10, 75, 10.1038/s41467-018-07948-7 · DOI
  18. Harnett, 1999, Molecular Cloning and Demonstration of an Aminopeptidase Activity in a Filarial Nematode Glycoprotein, Mol Biochem Parasitol, 104, 11, 10.1016/S0166-6851(99)00113-9 · DOI
  19. Stepek, 2002, Expression of the Filarial Nematode Phosphorylcholine-Containing Glycoprotein, ES62, Is Stage Specific, Parasitology, 125, 10.1017/S0031182002001920 · DOI
  20. Harnett, 1993, Acanthocheilonema Viteae: Phosphorylcholine Is Attached to the Major Excretory-Secretory Product via an N-Linked Glycan, Exp Parasitol, 77, 498, 10.1006/expr.1993.1113 · DOI
  21. Houston, 1996, Prevention of Attachment of Phosphorylcholine to a Major Excretory-Secretory Product of Acanthocheilonema Viteae Using Tunicamycin, J Parasitol, 82, 10.2307/3284169 · DOI
  22. Haslam, 1997, Characterisation of the Phosphorylcholine-Containing N-Linked Oligosaccharides in the Excretory-Secretory 62 kDa Glycoprotein of Acanthocheilonema Viteae, Mol Biochem Parasitol, 85, 53, 10.1016/S0166-6851(96)02807-1 · DOI
  23. North, 2019, Site-Specific Glycoproteomic Characterization of ES-62: The Major Secreted Product of the Parasitic Worm Acanthocheilonema Viteae, Glycobiology, 29, 10.1093/glycob/cwz035 · DOI
  24. Morelle, 2000, Phosphorylcholine-Containing N-Glycans of Trichinella Spiralis: Identification of Multiantennary lacdiNAc Structures, Glycobiology, 10, 10.1093/glycob/10.9.941 · DOI
  25. Wilson, 2016, Sweet Secrets of a Therapeutic Worm: Mass-Spectrometric N-Glycomic Analysis of Trichuris Suis, Anal Bioanal Chem, 408, 10.1007/s00216-015-9154-8 · DOI
  26. Hanneman, 2006, Isomer and Glycomer Complexities of Core GlcNAcs in Caenorhabditis Elegans, Glycobiology, 16, 10.1093/glycob/cwl011 · DOI
  27. Yan, 2015, Comparison of RP-HPLC Modes to Analyse the N-Glycome of the Free-Living Nematode Pristionchus Pacificus, Electrophoresis, 36, 10.1002/elps.201400528 · DOI
  28. Gerdt, 1999, Isolation, Characterization and Immunolocalization of Phosphorylcholine-Substituted Glycolipids in Developmental Stages of Caenorhabditis Elegans, Eur J Biochem, 266, 10.1046/j.1432-1327.1999.00937.x · DOI
  29. Grabitzki, 2008, The PCome of Caenorhabditis Elegans as a Prototypic Model System for Parasitic Nematodes: Identification of Phosphorylcholine-Substituted Proteins, Mol Biochem Parasitol, 161, 10.1016/j.molbiopara.2008.06.014 · DOI
  30. Houston, 2002, Investigation of the Nature of Potential Phosphorylcholine Donors for Filarial Nematode Glycoconjugates, Mol Biochem Parasitol, 123, 55, 10.1016/S0166-6851(02)00134-2 · DOI
  31. Cipollo, 2004, Biosynthesis In Vitro of Caenorhabditis Elegans Phosphorylcholine Oligosaccharides, Proc Natl Acad Sci USA, 101, 3404, 10.1073/pnas.0400384101 · DOI
  32. Houston, 1997, Studies on the Site and Mechanism of Attachment of Phosphorylcholine to a Filarial Nematode Secreted Glycoprotein, J Biol Chem, 272, 10.1074/jbc.272.3.1527 · DOI
  33. Houston, 2004, Structure and Synthesis of Nematode Phosphorylcholine-Containing Glycoconjugates, Parasitology, 129, 10.1017/S0031182004006171 · DOI
  34. Lal, 1990, Phosphocholine-Containing Antigens of Brugia Malayi Nonspecifically Suppress Lymphocyte Function, Am J Trop Med Hyg, 42, 56, 10.4269/ajtmh.1990.42.56 · DOI
  35. Harnett, 1993, Inhibition of Murine B Cell Proliferation and Down-Regulation of Protein Kinase C Levels by a Phosphorylcholine-Containing Filarial Excretory-Secretory Product, J Immunol (Baltimore Md 1950), 151, 10.4049/jimmunol.151.9.4829 · DOI
  36. Pineda, 2014, ES-62, a Therapeutic Anti-Inflammatory Agent Evolved by the Filarial Nematode Acanthocheilonema Viteae, Mol Biochem Parasitol, 194, 1, 10.1016/j.molbiopara.2014.03.003 · DOI · Paper page
  37. Deehan, 1998, A Phosphorylcholine-Containing Filarial Nematode-Secreted Product Disrupts B Lymphocyte Activation by Targeting Key Proliferative Signaling Pathways, J Immunol, 160, 10.4049/jimmunol.160.6.2692 · DOI
  38. Deehan, 2001, A Filarial Nematode-Secreted Phosphorylcholine-Containing Glycoprotein Uncouples the B Cell Antigen Receptor From Extracellular Signal-Regulated Kinase-Mitogen-Activated Protein Kinase by Promoting the Surface Ig-Mediated Recruitment of Src Homology 2 Domain-Containing Tyrosine Phosphatase-1 and Pac-1 Mitogen-Activated Kinase-Phosphatase, J Immunol, 166, 10.4049/jimmunol.166.12.7462 · DOI · Paper page
  39. Rzepecka, 2014, Small Molecule Analogues of the Immunomodulatory Parasitic Helminth Product ES-62 Have Anti-Allergy Properties, Int J Parasitol, 44, 10.1016/j.ijpara.2014.05.001 · DOI · Paper page
  40. Melendez, 2007, Inhibition of FcϵRI-Mediated Mast Cell Responses by ES-62, a Product of Parasitic Filarial Nematodes, Nat Med, 13, 10.1038/nm1654 · DOI
  41. Ball, 2013, Mast Cell Subsets and Their Functional Modulation by the Acanthocheilonema Viteae Product ES-62, Mast Cell Subsets and Their Functional Modulation by the Acanthocheilonema Viteae Product ES-62, J Parasitol Res, 2013, e961268, 10.1155/2013/961268 · DOI
  42. Bell, 2015, The Role of Individual Protein Kinase C Isoforms in Mouse Mast Cell Function and Their Targeting by the Immunomodulatory Parasitic Worm Product, ES-62, Immunol Lett, 168, 31, 10.1016/j.imlet.2015.09.001 · DOI
  43. Goodridge, 2007, Phosphorylcholine Mimics the Effects of ES-62 on Macrophages and Dendritic Cells, Parasite Immunol, 29, 10.1111/j.1365-3024.2006.00926.x · DOI · Paper page
  44. Goodridge, 2005, Immunomodulation via Novel Use of TLR4 by the Filarial Nematode Phosphorylcholine-Containing Secreted Product, ES-62, J Immunol, 174, 10.4049/jimmunol.174.1.284 · DOI
  45. Honda, 2005, IRF-7 Is the Master Regulator of Type-I Interferon-Dependent Immune Responses, Nature, 434, 10.1038/nature03464 · DOI
  46. Jin, 2007, Crystal Structure of the TLR1-TLR2 Heterodimer Induced by Binding of a Tri-Acylated Lipopeptide, Cell, 130, 10.1016/j.cell.2007.09.008 · DOI
  47. Honda, 2005, Spatiotemporal Regulation of MyD88–IRF-7 Signalling for Robust Type-I Interferon Induction, Nature, 434, 10.1038/nature03547 · DOI
  48. Hemmi, 2000, A Toll-Like Receptor Recognizes Bacterial DNA, Nature, 408, 10.1038/35047123 · DOI · Paper page
  49. Lumb, 2017, Dendritic Cells Provide a Therapeutic Target for Synthetic Small Molecule Analogues of the Parasitic Worm Product, ES-62, Sci Rep, 7, 1704, 10.1038/s41598-017-01651-1 · DOI
  50. Goodridge, 2001, Modulation of Macrophage Cytokine Production by ES-62, a Secreted Product of the Filarial Nematode Acanthocheilonema Viteae, J Immunol, 167, 10.4049/jimmunol.167.2.940 · DOI
  51. Zhou, 2014, Poly(I:C) Induces Antiviral Immune Responses in Japanese Flounder (Paralichthys Olivaceus) That Require TLR3 and MDA5 and Is Negatively Regulated by Myd88, PloS One, 9, e112918, 10.1371/journal.pone.0112918 · DOI
  52. Siednienko, 2011, Absence of MyD88 Results in Enhanced TLR3-Dependent Phosphorylation of IRF3 and Increased IFN-β and RANTES Production, J Immunol, 186, 10.4049/jimmunol.1003093 · DOI
  53. Alexopoulou, 2001, Recognition of Double-Stranded RNA and Activation of NF-κb by Toll-Like Receptor 3, Nature, 413, 10.1038/35099560 · DOI · Paper page
  54. Rzepecka, 2015, Prophylactic and Therapeutic Treatment With a Synthetic Analogue of a Parasitic Worm Product Prevents Experimental Arthritis and Inhibits IL-1β Production via NRF2-Mediated Counter-Regulation of the Inflammasome, J Autoimmun, 60, 59, 10.1016/j.jaut.2015.04.005 · DOI
  55. Suckling, 2018, Small Molecule Analogues of the Parasitic Worm Product ES-62 Interact With the TIR Domain of MyD88 to Inhibit Pro-Inflammatory Signalling, Sci Rep, 8, 2123, 10.1038/s41598-018-20388-z · DOI
  56. Pineda, 2015, From the Worm to the Pill, the Parasitic Worm Product ES-62 Raises New Horizons in the Treatment of Rheumatoid Arthritis, Lupus, 24, 10.1177/0961203314560004 · DOI
  57. Pineda, 2012, The Parasitic Helminth Product ES-62 Suppresses Pathogenesis in Collagen-Induced Arthritis by Targeting the Interleukin-17–Producing Cellular Network at Multiple Sites, Arthritis Rheum, 64, 10.1002/art.34581 · DOI
  58. Rodgers, 2015, Drug-Like Analogues of the Parasitic Worm-Derived Immunomodulator ES-62 Are Therapeutic in the MRL/Lpr Model of Systemic Lupus Erythematosus, Lupus, 24, 10.1177/0961203315591031 · DOI
  59. Vogel, 1999, Cutting Edge: Functional Characterization of the Effect of the C3H/HeJ Defect in Mice That Lack an Lps Gene: In Vivo Evidence for a Dominant Negative Mutation, J Immunol, 162, 10.4049/jimmunol.162.10.5666 · DOI
  60. Poltorak, 1998, Defective LPS Signaling in C3H/HeJ and C57BL/10ScCr Mice: Mutations in Tlr4 Gene, Science, 282, 10.1126/science.282.5396.2085 · DOI · Paper page
  61. Bovijn, 2012, Identification of Interaction Sites for Dimerization and Adapter Recruitment in Toll/interleukin-1 Receptor (TIR) Domain of Toll-Like Receptor 4, J Biol Chem, 287, 10.1074/jbc.M111.282350 · DOI
  62. Harnett, 2012, Receptor Usage by the Acanthocheilonema Viteae-Derived Immunomodulator, ES-62, Exp Parasitol, 132, 97, 10.1016/j.exppara.2011.09.001 · DOI
  63. Agrawal, 2001, Topology and Structure of the C1q-Binding Site on C-Reactive Protein, J Immunol, 166, 3998, 10.4049/jimmunol.166.6.3998 · DOI
  64. Agrawal, 1994, Probing the C1q-Binding Site on Human C-Reactive Protein by Site-Directed Mutagenesis, J Immunol, 152, 10.4049/jimmunol.152.11.5404 · DOI
  65. Kaplan, 1974, Interaction of C-Reactive Protein Complexes With the Complement System. I. Consumption of Human Complement Associated With the Reaction of C-Reactive Protein With Pneumococcal C-Polysaccharide and With the Choline Phosphatides, Lecithin and Sphingomyelin, J Immunol, 112
  66. Ricklin, 2010, Complement: A Key System for Immune Surveillance and Homeostasis, Nat Immunol, 11, 10.1038/ni.1923 · DOI · Paper page
  67. Ahmed, 2016, The Carbohydrate-Linked Phosphorylcholine of the Parasitic Nematode Product ES-62 Modulates Complement Activation, J Biol Chem, 291, 10.1074/jbc.M115.702746 · DOI
  68. Sjöwall, 2007, Solid-Phase Classical Complement Activation by C-Reactive Protein (CRP) Is Inhibited by Fluid-Phase CRP–C1q Interaction, Biochem Biophys Res Commun, 352, 10.1016/j.bbrc.2006.11.013 · DOI
  69. Houston, 2000, Presence of Phosphorylcholine on a Filarial Nematode Protein Influences Immunoglobulin G Subclass Response to the Molecule by an Interleukin-10-Dependent Mechanism, Infect Immun, 68, 10.1128/IAI.68.9.5466-5468.2000 · DOI
  70. Rocha, 2008, Protective Effect of an Extract From Ascaris Suum in Experimental Arthritis Models, Infect Immun, 76, 10.1128/IAI.01085-07 · DOI
  71. McInnes, 2003, A Novel Therapeutic Approach Targeting Articular Inflammation Using the Filarial Nematode-Derived Phosphorylcholine-Containing Glycoprotein ES-62, J Immunol, 171, 10.4049/jimmunol.171.4.2127 · DOI
  72. Rodgers, 2014, Protection Against Collagen-Induced Arthritis in Mice Afforded by the Parasitic Worm Product, ES-62, Is Associated With Restoration of the Levels of Interleukin-10-Producing B Cells and Reduced Plasma Cell Infiltration of the Joints, Immunology, 141, 10.1111/imm.12208 · DOI
  73. Pineda, 2014, ES-62 Protects Against Collagen-Induced Arthritis by Resetting Interleukin-22 Toward Resolution of Inflammation in the Joints, Arthritis Rheumatol, 66, 10.1002/art.38392 · DOI
  74. Doonan, 2019, The Parasitic Worm Product ES-62 Normalises the Gut Microbiota Bone Marrow Axis in Inflammatory Arthritis, Nat Commun, 10, 1554, 10.1038/s41467-019-09361-0 · DOI
  75. Brand, 2007, Collagen-Induced Arthritis, Nat Protoc, 2, 10.1038/nprot.2007.173 · DOI
  76. Pöllinger, 2011, Th17 Cells, Not IL-17+ γδ T Cells, Drive Arthritic Bone Destruction in Mice and Humans, J Immunol, 186, 10.4049/jimmunol.1003370 · DOI
  77. Harnett, 2014, The Parasitic Worm Product ES-62 Up-Regulates IL-22 Production by γδ T Cells in the Murine Model of Collagen-Induced Arthritis, Inflamm Cell Signal, 1, 10.14800/ics.308 · DOI
  78. Doonan, 2018, Protection Against Arthritis by the Parasitic Worm Product ES-62, and Its Drug-Like Small Molecule Analogues, Is Associated With Inhibition of Osteoclastogenesis, Front Immunol, 9, 10.3389/fimmu.2018.01016 · DOI · Paper page
  79. Rodgers, 2015, The Parasitic Worm Product ES-62 Targets Myeloid Differentiation Factor 88-Dependent Effector Mechanisms to Suppress Antinuclear Antibody Production and Proteinuria in MRL/lpr Mice, Arthritis Rheumatol, 67, 10.1002/art.39004 · DOI
  80. Aprahamian, 2015, The Immunomodulatory Parasitic Worm Product ES-62 Reduces Lupus-Associated Accelerated Atherosclerosis in a Mouse Model, Int J Parasitol, 45, 10.1016/j.ijpara.2014.12.006 · DOI
  81. Wilson, 2003, Hyporesponsiveness of Murine B Lymphocytes Exposed to the Filarial Nematode Secreted Product ES-62 In Vivo, Immunology, 109, 10.1046/j.1365-2567.2003.01661.x · DOI
  82. Rzepecka, 2013, The Helminth Product, ES-62, Protects Against Airway Inflammation by Resetting the Th Cell Phenotype, Int J Parasitol, 43, 10.1016/j.ijpara.2012.12.001 · DOI
  83. McSorley, 2012, Suppression of Type 2 Immunity and Allergic Airway Inflammation by Secreted Products of the Helminth Heligmosomoides Polygyrus, Eur J Immunol, 42, 10.1002/eji.201142161 · DOI
  84. Coltherd, 2016, The Parasitic Worm-Derived Immunomodulator, ES-62 and Its Drug-Like Small Molecule Analogues Exhibit Therapeutic Potential in a Model of Chronic Asthma, Sci Rep, 6, 19224, 10.1038/srep19224 · DOI
  85. Suckling, 2018, Synthetic Analogues of the Parasitic Worm Product ES-62 Reduce Disease Development in In Vivo Models of Lung Fibrosis, Acta Trop, 185, 10.1016/j.actatropica.2018.05.015 · DOI · Paper page
  86. Crowe, 2020, The Parasitic Worm Product ES-62 Promotes Health- and Life-Span in a High Calorie Diet-Accelerated Mouse Model of Ageing, PloS Pathog, 16, e1008391, 10.1371/journal.ppat.1008391 · DOI
  87. Lumb, 2019, Synthetic Small Molecule Analogues of the Immunomodulatory Acanthocheilonema Viteae Product ES-62 Promote Metabolic Homeostasis During Obesity in a Mouse Model, Mol Biochem Parasitol, 234, 111232, 10.1016/j.molbiopara.2019.111232 · DOI
  88. Doonan, 2018, Failure of the Anti-Inflammatory Parasitic Worm Product ES-62 to Provide Protection in Mouse Models of Type I Diabetes, Multiple Sclerosis, and Inflammatory Bowel Disease, Molecules, 23, 10.3390/molecules23102669 · DOI
  89. Pluijmert, 2020, Phosphorylcholine Antibodies Preserve Cardiac Function and Reduce Infarct Size by Attenuating the Post-Ischemic Inflammatory Response, JACC Basic Transl Sci, 5, 10.1016/j.jacbts.2020.09.012 · DOI
  90. de Vries, 2021, Identification of IgG1 Isotype Phosphorylcholine Antibodies for the Treatment of Inflammatory Cardiovascular Diseases, J Intern Med, 290, 10.1111/joim.13234 · DOI
  91. Frostegård, 2017, Antibodies Against Phosphorylcholine Among New Guineans Compared to Swedes: An Aspect of the Hygiene/Missing Old Friends Hypothesis, Immunol Invest, 46, 59, 10.1080/08820139.2016.1213279 · DOI
  92. Su, 2008, Natural Antibodies Against Phosphorylcholine as Potential Protective Factors in SLE, Rheumatology (Oxford), 47, 10.1093/rheumatology/ken120 · DOI
  93. Thiagarajan, 2020, Immunoglobulin G1 Antibodies Against Phosphorylcholine Are Associated With Protection in Systemic Lupus Erythematosus and Atherosclerosis: Potential Underlying Mechanisms, ACR Open Rheumatol, 2, 10.1002/acr2.11127 · DOI
  94. López, 2019, IgM Anti-Phosphorylcholine Antibodies Associate With Senescent and IL-17+ T Cells in SLE Patients With a Pro-Inflammatory Lipid Profile, Rheumatology, 59, 10.1093/rheumatology/kez264 · DOI
  95. Sun, 2018, IgM Antibodies Against Phosphorylcholine Promote Polarization of T Regulatory Cells From Patients With Atherosclerotic Plaques, Systemic Lupus Erythematosus and Healthy Donors, Atherosclerosis, 268, 36, 10.1016/j.atherosclerosis.2017.11.010 · DOI
  96. Thiagarajan, 2020, IgM Antibodies Against Malondialdehyde and Phosphorylcholine in Different Systemic Rheumatic Diseases, Sci Rep, 10, 11010, 10.1038/s41598-020-66981-z · DOI
  97. Ståhle, 2020, Therapeutic Antibody Against Phosphorylcholine Preserves Coronary Function and Attenuates Vascular (18)F-FDG Uptake in Atherosclerotic Mice, JACC Basic Transl Sci, 5, 10.1016/j.jacbts.2020.01.008 · DOI
  98. Que, 2018, Oxidized Phospholipids Are Proinflammatory and Proatherogenic in Hypercholesterolaemic Mice, Nature, 558, 10.1038/s41586-018-0198-8 · DOI · Paper page
  99. Lobo, 2017, Natural IgM and TLR Agonists Switch Murine Splenic Pan-B to “Regulatory” Cells That Suppress Ischemia-Induced Innate Inflammation via Regulating NKT-1 Cells, Front Immunol, 8, 10.3389/fimmu.2017.00974 · DOI
  100. Holodick, 2010, Immunoglobulin Secretion by B1 Cells: Differential Intensity and IRF4-Dependence of Spontaneous IgM Secretion by Peritoneal and Splenic B1 Cells, Eur J Immunol, 40, 10.1002/eji.201040545 · DOI
  101. Prieto, 2017, Development, Phenotype, and Function of Non-Conventional B Cells, Comp Immunol Microbiol Infect Dis, 54, 38, 10.1016/j.cimid.2017.08.002 · DOI
  102. Bhat, 1992, The Ontogeny and Functional Characteristics of Human B-1 (CD5+ B) Cells, Int Immunol, 4, 10.1093/intimm/4.2.243 · DOI
  103. Haury, 1997, The Repertoire of Serum IgM in Normal Mice Is Largely Independent of External Antigenic Contact, Eur J Immunol, 27, 10.1002/eji.1830270635 · DOI
  104. Masmoudi, 1990, All T15 Id-Positive Antibodies (But Not the Majority of VHT15+ Antibodies) Are Produced by Peritoneal CD5+ B Lymphocytes, Int Immunol, 2, 10.1093/intimm/2.6.515 · DOI
  105. Wilson, 2003, In Vivo Activation of Murine Peritoneal B1 Cells by the Filarial Nematode Phosphorylcholine-Containing Glycoprotein ES-62, Parasite Immunol, 25, 10.1111/j.1365-3024.2003.00650.x · DOI
  106. Ackerman, 2003, 19 Å Solution Structure of the Filarial Nematode Immunomodulatory Protein, ES-62, Biophys J, 84, 489, 10.1016/S0006-3495(03)74868-1 · DOI
  107. Egan, 2006, Lack of Immunological Cross-Reactivity Between Parasite-Derived and Recombinant Forms of Es-62, a Secreted Protein of Acanthocheilonema Viteae, Parasitology, 132, 10.1017/S0031182005009005 · DOI
  108. Harnett, 2010, How do Nematodes Transfer Phosphorylcholine to Carbohydrates, Trends Parasitol, 26, 10.1016/j.pt.2009.12.003 · DOI
  109. McVeigh, 2019, Can CRISPR Help in the Fight Against Parasitic Worms, eLife, 8, e44382, 10.7554/eLife.44382 · DOI
  110. Ball, 2018, IL-33/ST2 Signalling and Crosstalk With Fcϵri and TLR4 Is Targeted by the Parasitic Worm Product, ES-62, Sci Rep, 8, 4497, 10.1038/s41598-018-22716-9 · DOI · Paper page
  111. Lochnit, 2005, Searching New Targets for Anthelminthic Strategies: Interference With Glycosphingolipid Biosynthesis and Phosphorylcholine Metabolism Affects Development of Caenorhabditis Elegans, Int J Parasitol, 35, 10.1016/j.ijpara.2005.02.015 · DOI
  112. Houston, 2008, Gene Inactivation Confirms the Identity of Enzymes Involved in Nematode Phosphorylcholine-N-Glycan Synthesis, Mol Biochem Parasitol, 157, 88, 10.1016/j.molbiopara.2007.08.009 · DOI

Cited by

Sorted by citations

See all 8

Metadata

Authors
Buitrago, G., Duncombe-Moore, J., Harnett, M. M., & Harnett, W.
Venue
Frontiers in Tropical Diseases
Publisher
Frontiers Media SA
Published
2021-12-14
Volume
2
ISSN
2673-7515
DOI
10.3389/fitd.2021.769000
Cited by
8
References
3
Licence
creativecommons.org/licenses/by/4.0/ (vor)
Funders
Biotechnology and Biological Sciences Research Council

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: Mini Review: Structure and Function of Nematode Phosphorylcholine-Containing Glycoconjugates. https://app.cochat.ai/papers/10.3389/fitd.2021.769000
The paper
Buitrago, G., Duncombe-Moore, J., Harnett, M. M., & Harnett, W. (2021). Mini Review: Structure and Function of Nematode Phosphorylcholine-Containing Glycoconjugates. Frontiers in Tropical Diseases. https://doi.org/10.3389/fitd.2021.769000