Cloning, sequencing and immunological characterization of Dac g 3, a major allergen from Dactylis glomerata pollen

Guérin-Marchand, Claudine; Sénéchal, Hélène; Bouin, Anne-Pascale; Leduc-Brodard, Virginie; Taudou, G.; Weyer, A.; Peltre, Gabriel; David, B.

doi:10.1016/0161-5890(96)00015-6

Cited by 20 publications

(15 citation statements)

References 26 publications

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“…All following incubations were performed using phosphate-buffered saline (PBS) containing 0.3% Tween-20 (PBS-Tw) at room temperature (about 22°C). NC sheets were blocked for 1 h with PBS-Tw and incubated (overnight) with either grass pollen-allergic patient sera (1:10) or mouse mAb directed against D. glomerata allergen 4 (Dac g 4), revealing also Phl p 4 (1:1 500) [29], or rabbit polyclonal antibody directed against rDac g 3 (1:500)[ 30]. Phl p 3 can be easily identified by the polyclonal antibody directed against rDac g 3 due to their sequence homology in grass pollen family [31].…”

Section: Methodsmentioning

confidence: 99%

Modifications of Phleum pratense Grass Pollen Allergens following Artificial Exposure to Gaseous Air Pollutants (O3, NO2, SO2)

Rogerieux

Godfrin²,

Sénéchal³

et al. 2007

Int Arch Allergy Immunol

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Background: Air pollution is frequently proposed as a potential cause of the increased incidence of allergy in industrialised countries. Our objective was to investigate the impact of the major gaseous air pollutants on grass pollen allergens. Methods: Timothy grass pollen was exposed to ozone (O₃), nitrogen dioxide (NO₂) and sulphur dioxide (SO₂) alone or in combination. Allergen contents were analysed by 2-dimensional immunoblot using grass pollen-sensitive patient sera. Results: For O₃-treated pollen, immunoblotting showed an acidification of allergens Phl p 1b, Phl p 4, Phl p 5 and Phl p 6 and an IgE recognition decrease in Phl p 1, Phl p 2, Phl p 6 and Phl p 13. NO₂ exposure induced a decrease in Phl p 2, Phl p 5b and Phl p 6 recognition, and SO₂ treatment induced a decrease in Phl p 2, Phl p 6 and Phl p 13 recognition. Moreover, samples treated with a mix of NO₂/O₃ or NO₂/SO₂ showed a higher decrease in allergen content, compared with samples treated with only one pollutant. The O₃ acidification was also observed with the NO₂/O₃ mix. Conclusion: Exposure of pollen to gaseous pollutants induced a decrease in allergen detection in pollen extracts. This decrease could be due to a mechanical loss of allergens from the altered pollen grains and/or post-translational modifications affecting allergen recognition by IgE.

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Section: Methodsmentioning

confidence: 99%

Modifications of Phleum pratense Grass Pollen Allergens following Artificial Exposure to Gaseous Air Pollutants (O3, NO2, SO2)

Rogerieux

Godfrin²,

Sénéchal³

et al. 2007

Int Arch Allergy Immunol

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“…Group 2 allergens have since been cloned from L. perenne [63], Dactylis glomerata [64], P. pratense [60]and several other species (table 1). The only group 3 allergen cloned to date is that of D. glomerata [65]. …”

Section: Group 2 and Groupmentioning

confidence: 99%

“…Groups 2 and 3 comprise 10- to 12-kD non-glycosylated proteins of 95–98 amino acid residues [19, 58, 60, 61, 62, 64, 65]which exhibit 85–90% sequence identity between species. The sequence identities between the group 2 and group 3 allergens of L. perenne and D. glomerata are 60 and 64%, respectively.…”

Section: Group 2 and Groupmentioning

confidence: 99%

“…Nevertheless, the sequence of group 2 allergens and the corresponding part of group 1 allergens are sufficiently divergent to confer different surface properties and more or less distinct antibody recognition [67]. Cross-reactivity between group 1 and group 2 or 3 allergens has been demonstrated for rabbit antibodies and human IgG by inhibition experiments [65, 68, 69], but not for human IgE antibodies [60, 68]. In contrast, significant cross-reactivity for human IgE was found to exist between Lol p 2 and Lol p 3 [68].…”

Section: Group 2 and Groupmentioning

confidence: 99%

“…Members of groups 2 and 3 have been successfully expressed in E. coli [60, 63, 64, 65], and both the crystal and solution structures of recombinant (r)Phl p 2 have been determined [67, 70]. The molecule was found to be ellipsoid in shape and exhibit a stable 9-stranded β-sandwich resembling an Ig-fold, but without the specific features of the core packing observed in the immunoglobulin family.…”

Section: Group 2 and Groupmentioning

confidence: 99%

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Characteristics and Immunobiology of Grass Pollen Allergens

Andersson

Lidholm²

2003

Int Arch Allergy Immunol

315

311

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Grass pollens are one of the most important airborne allergen sources worldwide. About 20 species from five subfamilies are considered to be the most frequent causes of grass pollen allergy, and the allergenic relationships among them closely follow their phylogenetic relationships. The allergic immune response to pollen of several grass species has been studied extensively over more than three decades. Eleven groups of allergens have been identified and described, in most cases from more than one species. The allergens range from 6 to 60 kD in apparent molecular weight and display a variety of physicochemical properties and structures. The most complete set of allergens has so far been isolated and cloned from Phleum pratense (timothy grass) pollen. Based on the prevalence of IgE antibody recognition among grass pollen-sensitized individuals, several allergens qualify as major, but members of two groups, groups 1 and 5, have been shown to dominate the immune response to grass pollen extract. Isoform variation has been detected in members of several of the allergen groups, which in some cases can be linked to observed genetic differences. N-linked glycosylation occurs in members of at least three groups. Carbohydrate- reactive IgE antibodies have been attributed to grass pollen sensitization and found to cross-react with glycan structures from other allergen sources, particularly vegetable foods. Another cause of extensive cross-reactivity are the group 12 allergens (profilins), which belong to a family of proteins highly conserved throughout the plant kingdom and present in all tissues. Members of eight allergen groups have been cloned and expressed as recombinant proteins capable of specific IgE binding. This development now allows diagnostic dissection of the immune response to grass pollen with potential benefits for specific immunotherapy.

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Simultaneous quantitation of specific IgE against 20 purified allergens in allergic patients sera by checkerboard immunoblotting (CBIB)

Musu

Rabillon

Pelletier

et al. 1997

J. Clin. Lab. Anal.

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A simple technique, checkerboard immunoblotting (CBIB), is described for simultaneous quantitation of specific IgE antibodies against several allergens in human sera. Using as little as 50 μl of each of the 20 sera examined against 20 different allergens, it was possible in a single run to achieve 400 tests. To guarantee high specificity and sensitivity of the assay, this new application of CBIB employs purified allergens, cyanogen bromide‐activated nitrocellulose membrane, and Phosphorimager technology. Results are expressed both qualitatively (five classes) and quantitatively in kilo units per liter equilibrated against the World Health Organization (WHO) standard for IgE. There was excellent agreement between the results of CBIB and the results of Pharmacia Cap System, an alternative method widely used for measuring serum‐specific IgE. The CBIB method certainly could be useful in any laboratory interested in allergy clinical research for easy screening and relative quantitation of allergen‐specific human IgE. J. Clin. Lab. Anal. 11:357–362, 1997.© 1997 Wiley‐Liss, Inc.

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Cloning, sequencing and immunological characterization of Dac g 3, a major allergen from Dactylis glomerata pollen

Cited by 20 publications

References 26 publications

Modifications of <i>Phleum pratense</i> Grass Pollen Allergens following Artificial Exposure to Gaseous Air Pollutants (O<sub>3</sub>, NO<sub>2</sub>, SO<sub>2</sub>)

Modifications of <i>Phleum pratense</i> Grass Pollen Allergens following Artificial Exposure to Gaseous Air Pollutants (O<sub>3</sub>, NO<sub>2</sub>, SO<sub>2</sub>)

Characteristics and Immunobiology of Grass Pollen Allergens

Simultaneous quantitation of specific IgE against 20 purified allergens in allergic patients sera by checkerboard immunoblotting (CBIB)

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