Mapping of an allergenically important determinant of grass group I allergens

Hiller, Kara M.; Esch, Robert E.; Klapper, David G.

doi:10.1016/s0091-6749(97)70246-x

Cited by 27 publications

(15 citation statements)

References 14 publications

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“…(Petersen et al, 1993(Petersen et al, , 1995(Petersen et al, , 1997Knox and Suphioglu, 1996b;Hiller et al, 1997). In maize, we found two divergent classes of Zea m 1 cDNAs with quite different protein sequence (only approximately 62% identical to each other).…”

Section: Zea M 1 Isoformsmentioning

confidence: 78%

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Purification and Characterization of Four β-Expansins (Zea m 1 Isoforms) from Maize Pollen

et al. 2003

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(P.A.B., C.V.).Four proteins with wall extension activity on grass cell walls were purified from maize (Zea mays) pollen by conventional column chromatography and high-performance liquid chromatography. Each is a basic glycoprotein (isoelectric point ϭ 9.1-9.5) of approximately 28 kD and was identified by immunoblot analysis as an isoform of Zea m 1, the major group 1 allergen of maize pollen and member of the ␤-expansin family. Four distinctive cDNAs for Zea m 1 were identified by cDNA library screening and by GenBank analysis. One pair (GenBank accession nos. AY104999 and AY104125) was much closer in sequence to well-characterized allergens such as Lol p 1 and Phl p 1 from ryegrass (Lolium perenne) and Phleum pretense, whereas a second pair was much more divergent. The N-terminal sequence and mass spectrometry fingerprint of the most abundant isoform (Zea m 1d) matched that predicted for AY197353, whereas N-terminal sequences of the other isoforms matched or nearly matched AY104999 and AY104125. Highly purified Zea m 1d induced extension of a variety of grass walls but not dicot walls. Wall extension activity of Zea m 1d was biphasic with respect to protein concentration, had a broad pH optimum between 5 and 6, required more than 50 g mL Ϫ1 for high activity, and led to cell wall breakage after only approximately 10% extension. These characteristics differ from those of ␣-expansins. Some of the distinctive properties of Zea m 1 may not be typical of ␤-expansins as a class but may relate to the specialized function of this ␤-expansin in pollen function.Expansins were first identified a decade ago as mediators of acid-induced plant cell wall extension in cucumber (Cucumis sativus) hypocotyls and oat (Avena sativa) coleoptiles (McQueen-Mason et al., 1992;Li et al., 1993) and since then have been implicated in many aspects of plant growth and development, including cell expansion, leaf organogenesis and phyllotaxy, fruit ripening, root growth, particularly during drought, cell wall disassembly, and penetration of pollen tubes in grass species (for review, see Cosgrove, 2000;Cosgrove et al., 2002). Currently, two families of expansins, named EXP (␣-expansins) and EXPB (␤-expansins), have been identified based on protein activity and sequence analysis (Shcherban et al., 1995;Cosgrove et al., 2002;Li et al., 2002). The rice (Oryza sativa) and Arabidopsis genomes also contain a small family of related genes (see http://www.bio.psu.edu/expansins/) that we have named EXPL (expansin-like) and a more distant gene named EXPR (expansin-related). It is unknown whether the proteins encoded by these distantly related genes have expansin's characteristic activity, namely a rapid induction of cell wall extension and an increase in wall stress relaxation.Although there are now many reports characterizing expansin gene expression, relatively few studies have examined the activity of expansin proteins. It seems that ␣-expansins are ubiquitous to land plants and loosen cell walls without breakdown of the major wall polysaccharides (...

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Section: Zea M 1 Isoformsmentioning

confidence: 78%

“…4, C-E) using monoclonal antibody (McAb) against Lol p 1 (antisite D, where the epitope is defined by the Lol p 1 peptide STWYGKPTGAGPK; Hiller et al, 1997; see also the annotation of the sequence alignment in Fig. 1).…”

Section: Identification Of Zea M 1 By Immunoblot and Amino Acid Sequementioning

confidence: 99%

Purification and Characterization of Four β-Expansins (Zea m 1 Isoforms) from Maize Pollen

et al. 2003

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“…Of note, only 3/40 children were positive to the mold mix extract using skin prick testing (serum testing not performed, data not shown). On the other hand, the northern grass pollen used for skin testing contain antigens that have been shown to be largely present in timothy grass [11, 12] which speaks against the argument that antigenic differences solely account for the observed discrepancies. Likewise, Dermatophagoides farinae (Der f1) and Dermatophagoides pteronyssinus (Der p1) have high sequence analogy, in agreement with their high cross reactivity [13].…”

Section: Discussionmentioning

confidence: 99%

Discordance between aeroallergen specific serum IgE and skin testing in children younger than 4 years

Vos

Nazari

Ferastraoaru

et al. 2013

Annals of Allergy, Asthma & Immunology

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Background Atopic sensitization to aeroallergens in early life has been shown to be a strong risk factor for developing persisting asthma in young children with recurrent wheeze. Objective The aim of this study was to assess the yield of skin prick test (SPT) compared to allergen specific serum IgE testing (sIgE) at identifying aeroallergen sensitization in atopic children < 4 years of age. Methods Concordance between SPT (Greer Laboratories, ComforTen™) and allergen specific sIgE (Immulite 2000™) for 7 common aeroallergens was analyzed in forty atopic inner-city children, 18–48 months of age (mean 36 +/− 9 months) with recurrent wheezing, family history of asthma and/or eczema. Results In 80% of children one or more allergen sensitizations would have been missed if only SPT had been performed, and in 38% of children one or more sensitizations would have been missed if only serum IgE testing had been performed. Agreement and between SPT and sIgE test was fair for most allergens (kappa between −0.04 and 0.50), as was correlation between sIgE levels and SPT grade (rho between 0.21 and 0.55). Children with high total sIgE (≥300 kU/l) were more likely to have sIgE positive tests with negative corresponding skin test (p=0.025). Conclusions Our study showed significant discordance between allergen specific SPT and sIgE testing results for common aeroallergens, suggesting that both SPT and sIgE testing should be done when diagnosing allergic sensitization in young children at high risk of asthma.

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“…Other modifications present in group 1 allergens include hydroxyproline residues at positions 5 and 8 in most species [22, 23, 30, 46]and possible phosphorylation at one or several of seven serine and threonine residues located within potential phosphorylation sites [23, 47]. …”

Section: Groupmentioning

confidence: 99%

Characteristics and Immunobiology of Grass Pollen Allergens

Andersson

Lidholm²

2003

Int Arch Allergy Immunol

312

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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Mapping of an allergenically important determinant of grass group I allergens

Cited by 27 publications

References 14 publications

Purification and Characterization of Four β-Expansins (Zea m 1 Isoforms) from Maize Pollen

Purification and Characterization of Four β-Expansins (Zea m 1 Isoforms) from Maize Pollen

Discordance between aeroallergen specific serum IgE and skin testing in children younger than 4 years

Characteristics and Immunobiology of Grass Pollen Allergens

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