Phosphorylcholine-containing N-glycans of Trichinella spiralis: identification of multiantennary lacdiNAc structures

Morelle, Willy; Haslam, Stuart M.; Olivier, Verena; Appleton, Judith A.; Morris, Howard R.; Dell, Anne

doi:10.1093/glycob/10.9.941

Cited by 71 publications

(56 citation statements)

References 42 publications

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“…These data suggest that only some of the cross-reacting epitopes contained in CLE glycoproteins are O-glycans in nature. Other immunodominant epitopes (e.g., phosphorylcholine), present on Nglycan structures (29), are also readily released by alkaline treatment (unpublished results), thus ruling out the possibility that this epitope is involved in the residual cross-reactions observed with filariae and Dracunculus after alkaline treatment. Furthermore, in addition to the specificity problem, the sensitivity of ELISA with O-deglycosylated CLE dropped drastically after alkaline treatment, probably because of the destruction of relevant Trichinella epitopes contained in CLE preparations.…”

Section: Discussionmentioning

confidence: 95%

Evaluation ofTrichinella spiralisLarva Group 1 Antigens for Serodiagnosis of Human Trichinellosis

et al. 2004

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To identify Trichinella antigens suitable for high-specificity and high-sensitivity serodiagnosis of human trichinellosis, we evaluated assays using four antigens: (i) crude first-stage larval extract (CLE), (ii) Odeglycosylated CLE, (iii) tyvelose-bearing antigens (Trichinella spiralis larva group 1 [TSL-1] antigens) purified by US4 affinity chromatography and coupled directly to enzyme-linked immunosorbent assay (ELISA) plates (pTSL-1 antigens), and (iv) TSL-1 antigens immobilized on ELISA plates with the monoclonal antibody (MAb) US4 (cTSL-1 antigens). Assays using these antigens were compared by analysis of sera from healthy individuals (n ‫؍‬ 224) (group 1), individuals with noninfectious intestinal pathologies (n ‫؍‬ 114) (group 2), individuals with other parasitic infections (n ‫؍‬ 107) (group 3), and individuals with confirmed trichinellosis (n ‫؍‬ 42) (group 4). Our results indicate that capture ELISA using cTSL-1 antigens is the most effective method for serodiagnosis of human trichinellosis; this was the only method showing 100% specificity and 100% sensitivity at the patent stage of the infection, and it was also the most sensitive for sera obtained prior to patency in indirect immunofluorescence (IIF). Indirect ELISA with pTSL-1 antigens was also 100% specific but was slightly less sensitive, particularly with sera obtained before IIF patency. Inhibition ELISA with MAb US4 indicated (i) that in Trichinella-infected patients the immune response to TSL-1 antigens is directed mostly against tyvelose-containing epitopes (mean of 84.2% of total anti-TSL-1 immunoglobulin G1 [IgG1] antibody response [range, 51.3 to 97.6%]) and (ii) that in most individuals a large proportion of anti-CLE IgG1 antibodies (mean, 49.5%; range, 7.3 to 92.6%) are directed against tyvelose epitopes.

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Section: Discussionmentioning

confidence: 95%

Evaluation ofTrichinella spiralisLarva Group 1 Antigens for Serodiagnosis of Human Trichinellosis

et al. 2004

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“…None of these structures were core ␣(1,3) fucosylated. For distantly related nematodes like the filaria Acanthocheilonema viteae (13), Trichinella spiralis (23), and the free-living nematode Caenorhabditis elegans (4), PC has been reported to be linked to an N-acetylhexosamine, most likely GlcNAc. Because of the reactivity of GP300 with WGA, it seems plausible that in D. viviparus PC is also attached to a GlcNAc residue.…”

Section: Discussionmentioning

confidence: 99%

Antibodies Elicited by the Bovine Lungworm,Dictyocaulus viviparus, Cross-React with Platelet-Activating Factor

et al. 2007

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Parasite N-glycans may play an important role in helminth infections. As antibodies from Dictyocaulus viviparus-infected calves strongly react with N-glycans, we investigated the characteristics of the major immunodominant glycoprotein (GP300) of this parasite. Probing of worm extracts with various lectins demonstrated unique binding of GP300 to wheat germ agglutinin. Analysis of lectin-purified GP300 revealed that the glycan was substituted with phosphorylcholine and reacted with the phosphorylcholine-specific antibody TEPC-15. Competitive enzyme-linked immunosorbent assay with GP300-coated plates and GP300-specific immunoglobulin G (IgG) in conjunction with free phosphorylcholine or TEPC-15 demonstrated that antibodies from infected calves recognized phosphorylcholine on GP300. Additional assays showed that these antibodies cross-reacted with the phosphorylcholine moiety present on platelet-activating factor (PAF; 1-O-alkyl-2-acetyl-snglycero-3-phosphocholine), a proinflammatory mediator of the host. Heavily infected calves contained high levels of serum GP300-specific IgG1 but low levels of IgA and IgG2 and showed a reduced influx of eosinophils in the lungs, all consistent with a neutralization of PAF activity. In conclusion, we demonstrated that D. viviparus infection elicits GP300-specific antibodies that cross-react with PAF and may neutralize PAF function, thus limiting the development of a protective response as well as parasite-induced host pathology.

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“…It is well established that many N-linked glycans of nematodes are modified by the addition of phosphorylcholine (PC) (10,16,37) and that this modification underlies some of the immunological effects exerted by nematode glycoproteins on the immune system (19,20,25). For example, PC-containing glycoprotein ES-62 secreted by the nematode Acanthochelo- Our present data do not discern whether the Th2-skewing influence of nematode antigens is attributable to the carbohydrate moieties or to the attached PC residues or to both.…”

Section: Discussionmentioning

confidence: 99%

Both Free-Living and Parasitic Nematodes Induce a Characteristic Th2 Response That Is Dependent on the Presence of Intact Glycans

et al. 2004

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Infection with parasitic nematodes is characterized by the induction of a profound type 2 immune response. We have studied the role of glycans in the induction of the skewed type 2 response by antigens of the parasitic nematode Brugia malayi as well as the free-living nematode Caenorhabditis elegans. Lymph node cells from BALB/c mice immunized with soluble extracts of the two nematodes showed distinct antigen-specific proliferation and cytokine production; however, both nematodes induced antigen-specific interleukin 4 (IL-4) production, demonstrating that the induction of a biased type 2 response is not unique to parasitic nematodes. Sodium periodate-treated soluble extracts of both nematodes consistently induced significantly less IL-4 production than the respective mock-treated extracts, indicating that glycans play a critical role in the induction of the Th2 immune response by these nematodes. The glycan-dependent induction of the Th2-potentiating cytokine IL-4 occurs by 72 h postinoculation. Our data suggest that glycan determinants common to nematodes act as ligands, displaying distinct molecular patterns that trigger the immune system to launch a biased Th2 immune response upon exposure to these organisms or their products. Further, the similarity of our findings to those for Schistosoma mansoni egg antigen is striking considering the enormous phylogenetic distance between nematodes and trematodes. These data thus have important implications for how the mammalian host responds to widely divergent metazoan invaders and suggest that the powerful C. elegans model system can be used to address these questions.

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Phosphorylcholine-containing N-glycans of Trichinella spiralis: identification of multiantennary lacdiNAc structures

Cited by 71 publications

References 42 publications

Evaluation ofTrichinella spiralisLarva Group 1 Antigens for Serodiagnosis of Human Trichinellosis

Evaluation ofTrichinella spiralisLarva Group 1 Antigens for Serodiagnosis of Human Trichinellosis

Antibodies Elicited by the Bovine Lungworm,Dictyocaulus viviparus, Cross-React with Platelet-Activating Factor

Both Free-Living and Parasitic Nematodes Induce a Characteristic Th2 Response That Is Dependent on the Presence of Intact Glycans

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