Overview on denominated allergens

Liebers, Verena; Sander, I.; Kampen, V. van; Raulf‐Heimsoth, Monika; Rozynek, P.; Baur, Xaver

doi:10.1111/j.1365-2222.1996.tb00570.x

Cited by 39 publications

(21 citation statements)

References 267 publications

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“…Ole e 1, Par j 1, etc.) [11, 12]would complete this component-resolved diagnosis [37]. The allergenic molecule-based diagnosis would also help in the correct choice of an SIT treatment that should include all the allergenic extracts relevant for the patient, until allergenic molecules are available for the immunotherapy of allergic diseases [37].…”

Section: Discussionmentioning

confidence: 99%

“…In the last decades, an increasing number of purified natural or recombinant allergens have been fully characterized in terms of physicochemical characteristics, biochemical properties, sequence homology and taxonomy [11, 12]. Several studies focused the possible replacement of the allergenic extracts with the recombinant allergenic molecules for diagnostic purposes [13, 14, 15, 16].…”

Section: Introductionmentioning

confidence: 99%

“…The molecules chosen for the study were rPhl p 5, rBet v 1, rBet v 2, rJun o 2 and CCDs. Phl p 5 is an allergenic protein from Phleum pratense (timothy grass) with a high level of homology with proteins (denominated group 5 allergens) present only in the grass family [11, 14]. Bet v 1, the major allergen of birch, has a high level of homology with other proteins from species of the Betulaceae, Corylaceae and Fagaceae families, all belonging to the Fagales order [20].…”

Section: Introductionmentioning

confidence: 99%

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Multiple Pollen Sensitization: A Molecular Approach to the Diagnosis

Mari¹

2001

Int Arch Allergy Immunol

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Background: Sensitization to multiple pollen species is a frequent diagnostic event. Several allergenic molecules with a high level of homology have been identified in divergent pollen families and named panallergens. Methods: We sought to define the criteria to evaluate the prevalence of the multiple pollen sensitization, to identify specific markers of this condition, and to correlate them with the underlying allergic disease. Patients presenting an allergic respiratory disease underwent skin testing with 23 pollens. Patients fulfilling predefined selection criteria were grouped and classified as having multiple pollen sensitization. Patients in each subgroup were tested for IgE to rBet v 2, rJun o 2, rBet v 1, rPhl p 5 and bromelain. Demographical, allergological and clinical data were recorded in the subgroup of patients with multiple pollen sensitization. Results: Seventeen percent of the pollen-sensitized patients formed the multiple pollen-sensitized subgroup. These subjects were positive for most of the pollen species tested regardless of known exposure to them. None of the subjects sensitized to less than six pollen species were positive to panallergens, whereas 55% of the sera of the multiple pollen-sensitized group were positive to rBet v 2, and 15% to rJun o 2. IgE to rBet v 1 and rPhl p 5 were found positive in all the subgroups. Age, gender, bronchial asthma, oral allergy syndrome, skin test reactivity and previous specific immunotherapy differed significantly when these two subsets were considered. Conclusions: Allergy diagnosis based on allergenic molecules is crucial in the patient with multiple pollen sensitization. This condition appears to be determined by the sensitization to defined allergenic components (panallergens) rather than by pollen of multiple species as such. Detection of IgE to nonpanallergenic molecules allows to identify more relevant allergenic sources. Clinical aspects of the underlying allergic disease (e.g. asthma and oral allergy syndrome) seem to be differently related to IgE reactivity to panallergens.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Multiple Pollen Sensitization: A Molecular Approach to the Diagnosis

Mari¹

2001

Int Arch Allergy Immunol

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“…However, allergies arise in response to certain otherwise innocuous proteins, allergens. The list of denominated allergens contains more than 170 proteins from different species (2). These proteins are structurally and functionally a heterogeneous group, including hydrolytic enzymes, enzyme inhibitors, and transport molecules, but there are also a number of proteins without a known function (3).…”

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confidence: 99%

Probing the Molecular Basis of Allergy

Rouvinen

Rautiainen

Virtanen

et al. 1999

Journal of Biological Chemistry

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“…For example, it has been reported that the IgE–binding epitope sequences of a Schistosoma japonicum antigen exhibited similarities with those of known allergens, including lipocalins [108]. In addition, several allergens appear to be conserved in evolution [109]. For example, some allergenic proteins of Aspergillus fumigatus have been reported to show a high degree of sequence identity and similarity to human counterparts [110].…”

Section: Immune Defense System and Allergymentioning

confidence: 99%

Important Animal Allergens Are Lipocalin Proteins: Why Are They Allergenic?

Virtanen¹,

Zeiler²,

Mäntyjärvi³

1999

Int Arch Allergy Immunol

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Major respiratory allergens of dogs, mice, rats, horses and cows belong to the lipocalin group of proteins. The sequence identity of lipocalins is often less than 20%, but they contain between one and three structurally conserved regions and their three–dimensional structures are similar. Lipocalins share common biological functions, predominantly related to the transport of small hydrophobic molecules, such as vitamins and pheromones. Immune reactivity to lipocalin allergens is not well known. In Bos d 5, the IgE–binding epitopes are spread along the molecule, whereas in Bos d 2, the C terminus appears to contain the human B cell epitopes. Bos d 5 contains several murine T cell epitopes. No information is available on human T cell epitopes. The maximal number of epitopes an allergic patient’s T cells could recognize in Bos d 2 was five. Three of the epitopes were colocalized in the structurally conserved regions of lipocalins. Interestingly, one of the epitopes was recognized by the T cells of all patients and the computer predictions suggested that there would be an epitope in the corresponding parts of human endogenous lipocalins. The proliferative responses of peripheral blood mononuclear cells of Bos d 2–allergic subjects to Bos d 2 were weak. The T cell response was Th2–dominated. To explain these observations, we have proposed that the allergenicity of lipocalins may be a consequence of molecular mimicry between lipocalin allergens and endogenous lipocalins at the T cell level.

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Overview on denominated allergens

Abstract: Allergen identification and characterization (molecular weight, amino acid sequenee, structural data)

Cited by 39 publications

References 267 publications

Multiple Pollen Sensitization: A Molecular Approach to the Diagnosis

Multiple Pollen Sensitization: A Molecular Approach to the Diagnosis

Probing the Molecular Basis of Allergy

Important Animal Allergens Are Lipocalin Proteins: Why Are They Allergenic?

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