Identification by immunoblot of venom glycoproteins displaying immunoglobulin E‐binding <i>N</i>‐glycans as cross‐reactive allergens in honeybee and yellow jacket venom

Hemmer, Wolfgang; Focke, Margarete; Kolarich, Daniel; Dalik, I; Götz, M.; Jarisch, Reinhart

doi:10.1111/j.1365-2222.2004.01897.x

Cited by 101 publications

(104 citation statements)

References 39 publications

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“…Previous studies have shown that venom-allergic individuals can develop IgE antibodies against specific carbohydrate structures. The N-glycan structures containing -1,3-linked fucose residues at the glycan core have been suggested to be involved in this type of IgE-mediated cross-reactivity and thus are considered to be a major cause of in vitro double positivity in honeybee and vespid-allergic individuals (Hemmer et al, 2001(Hemmer et al, , 2004. Interestingly, in the present study only one site at Asn99 was found to carry this type of N-glycan.…”

Section: N-glycosylation Of Natural Ves Vmentioning

confidence: 40%

“…However, as far as we know, the sugar moieties of rApi m 2 have not yet been modelled and/or characterized. In contrast, it has been shown that natural Api m 2 is glycosylated at Asn263 with a Man 6(Man 3)Man 4GlcNAc 4(Fuc 3)GlcNAc -Asn type oligosaccharide containing six or seven sugar rings (Hemmer et al, 2004;Kolarich & Altmann, 2000). A corresponding glycosylation site is not found in Ves v 2.…”

Section: N-glycosylation Of Natural Ves Vmentioning

confidence: 94%

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Structure of recombinant Ves v 2 at 2.0 Å resolution: structural analysis of an allergenic hyaluronidase from wasp venom

Skov

Seppälä

Coen

et al. 2006

Acta Crystallogr D Biol Crystallogr

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Wasp venom from Vespula vulgaris contains three major allergens: Ves v 1, Ves v 2 and Ves v 5. Here, the cloning, expression, biochemical characterization and crystal structure determination of the hyaluronidase Ves v 2 from family 56 of the glycoside hydrolases are reported. The allergen was expressed in Escherichia coli as an insoluble protein and refolded and purified to obtain full enzymatic activity. Three N‐glycosylation sites at Asn79, Asn99 and Asn127 were identified in Ves v 2 from a natural source by enzymatic digestions combined with MALDI–TOF mass spectrometry. The crystal structure of recombinant Ves v 2 was determined at 2.0 Å resolution and reveals a central (β/α)7 core that is further stabilized by two disulfide bonds (Cys19–Cys308 and Cys185–Cys197). Based on sequence alignments and structural comparison with the honeybee allergen Api m 2, it is proposed that a conserved cavity near the active site is involved in binding of the substrate. Surface epitopes and putative glycosylation sites have been compared with those of two other major group 2 allergens from Apis mellifera (honeybee) and Dolichovespula maculata (white‐faced hornet). The analysis suggests that the harboured allergic IgE‐mediated cross‐reactivity between Ves v 2 and the allergen from D. maculata is much higher than that between Ves v 2 and the allergen from A. mellifera.

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Section: N-glycosylation Of Natural Ves Vmentioning

confidence: 40%

Section: N-glycosylation Of Natural Ves Vmentioning

confidence: 94%

Structure of recombinant Ves v 2 at 2.0 Å resolution: structural analysis of an allergenic hyaluronidase from wasp venom

Skov

Seppälä

Coen

et al. 2006

Acta Crystallogr D Biol Crystallogr

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“…Venoms of the yellow jacket species considered so far contain three major allergens: antigen 5 (Ag5 or Ves x 5), phospholipase (PLA or Ves x 1) and hyaluronidase (Hyase or Ves x 2), the latter being a glycoprotein [2][3][4][5][6]. Other proteins such as Vmac1 and Vmac3 have additionally been described as minor allergens from V. maculifrons [7].…”

Section: Introductionmentioning

confidence: 99%

A proteomic study of the major allergens from yellow jacket venoms

et al. 2007

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The venoms of stinging insects belong to the most dangerous allergen sources and can cause fatal anaphylactic reactions. Reliable prediction of a patient's risk to anaphylactic reactions is vital, and diagnosis requires the knowledge of the relevant allergens. Recently, a new hyaluronidase -like glycoprotein from Vespula vulgaris (Ves v 2b) was identified. This led us to investigate hyaluronidases and also other major allergens from V. germanica and four additional Vespula species. By MALDI-Q-TOF-MS, the new hyaluronidase-like protein was shown to be the major component of the 43-kDa band in all Vespula species studied. LC-ESI-Q-TOF-MS/MS sequencing of Ves g 2a and Ves g 2b facilitated the cloning of their cDNA. Ves v 2b and Ves g 2b turned out to be essentially identical on protein level. Whereas the less abundant "a" form displayed enzymatic activity, the new "b" homologue did not. This is probably caused by amino acid exchanges in the active site, and it raises questions about the physiological role of this protein. Sequence comparisons by MS/MS of antigen 5 and phospholipases from V. vulgaris, germanica, maculifrons, pensylvanica, flavopilosa and squamosa revealed the latter as a taxonomic outlier and led to the discovery of several not previously reported amino acid differences.

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“…In the context of our results it is noteworthy that core N-glycans modified with (α1-3)-Fuc and/or (β1-2)-Xyl residues in honeybee (HB) and vespid venoms [23] are proposed as immunogens responsible for cross-sensitisation to HB and yellow jacket (YJ). Whether protection of gpMuc against Echis carinatus venom depends upon the presence of the same (α1-3)-Fuc and/or (β1-2)-Xyl residues is now under study in our laboratories.…”

Section: Discussionmentioning

confidence: 79%

Structural characterization of the N-glycans of gpMuc from Mucuna pruriens seeds

et al. 2006

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Mucuna pruriens seeds are used in some countries as a human prophylactic oral anti-snake remedy. Aqueous extracts of M. pruriens seeds possess in vivo activity against cobra and viper venoms, and protect mice against Echis carinatus venom. It was recently demonstrated that the seed immunogen generating the antibody that cross-reacts with the venom proteins is a multiform glycoprotein (gpMuc), and the immunogenic properties of gpMuc seemed to mainly reside in its glycan chains. In the present study, gpMuc was found to contain only N-glycans. Part of the N-glycans could be released with peptide-(N 4 -(N -acetyl-β-glucosaminyl)asparagine amidase F (PNGase F-sensitive Nglycans); the PNGase F-resistant N-glycans were PNGase A-sensitive. The oligosaccharides released were analyzed by a combination of MALDI-TOF mass spectrometry, HPLC profiling of 2-aminobenzamide-labelled derivatives and 1 H NMR spectroscopy. The PNGase F-sensitive N-glycans comprised a mixture of oligomannose-type structures ranging from Man 5 GlcNAc 2 to Man 9 GlcNAc 2 , and two xylosylated

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Identification by immunoblot of venom glycoproteins displaying immunoglobulin E‐binding N‐glycans as cross‐reactive allergens in honeybee and yellow jacket venom

Cited by 101 publications

References 39 publications

Structure of recombinant Ves v 2 at 2.0 Å resolution: structural analysis of an allergenic hyaluronidase from wasp venom

Structure of recombinant Ves v 2 at 2.0 Å resolution: structural analysis of an allergenic hyaluronidase from wasp venom

A proteomic study of the major allergens from yellow jacket venoms

Structural characterization of the N-glycans of gpMuc from Mucuna pruriens seeds

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