Article
Prevalence and clinical relevance of specific immunoglobulin E to pollen caused by sting- induced specific immunoglobulin E to cross-reacting carbohydrate determinants in Hymenoptera venoms.
Department of Internal Medicine, Division of Allergy and Clinical Immunology, University Hospital Gasthuisberg, Leuven, Belgium.
Clinical & Experimental Allergy (impact factor:
5.03).
05/2005;
35(4):441-7.
DOI:10.1111/j.1365-2222.2005.02217.x
pp.441-7
Source: PubMed
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Citations (0)
- Cited In (6)
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Article: Determinants of food allergy.
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ABSTRACT: Food allergy is an emerging epidemic in the United States and the Western world. The determination of factors that make certain foods allergenic is still not clearly understood. Only a tiny fraction of thousands of proteins and other molecules is responsible for inducing food allergy. In this review, the authors present 3 examples of food allergies with disparate clinical presentations: peanut, soy, and mammalian meat. The potential relationships between allergen structure and function, emphasizing the importance of cross-reactive determinants, immunoglobulin E antibodies to the oligosaccharides, and the immune responses induced in humans are discussed.Immunology and allergy clinics of North America 02/2012; 32(1):11-33. · 3.18 Impact Factor -
Article: Clinical Features and the Diagnostic Value of Component Allergen-Specific IgE in Hymenoptera Venom Allergy.
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ABSTRACT: Although patient history is vital for the diagnosis of hymenoptera venom allergy, specific IgE detection is also important to identify the culprit insect and monitor the effect of immunotherapy. We evaluated the diagnostic value of serum-specific IgE detection of hymenoptera venom component allergens and documented changes in allergen-specific IgE after immunotherapy. Fifty-six hymenoptera venom allergy patients receiving venom immunotherapy were recruited from Ajou University Hospital, Korea. The clinical manifestations of the patients were noted, and serum-specific IgE detection was performed, using conventional venom extracts as well as component allergens. Data were analyzed retrospectively. A total of 35 (62.5%) patients were male, and 33 (73.3%) patients were atopic. The mean patient age was 44.9±13.8 years. Localized reactions occurred in 23.2% of patients, and systemic reactions occurred in 76.8%. The most common clinical manifestations included skin involvement, such as urticaria and angioedema, and respiratory involvement. Yellow jackets were the most frequent culprit insect, followed by yellow hornets, white-faced hornets, honeybees, and paper wasps, as determined at the time of diagnosis. Double sensitization to both Apidae and Vespidae species was detected in 70.9% of patients. The positive predictive values (PPV) of rVes v 5-specific and rPol d 5-specific IgE detection were 85.7% and 87.5%, respectively, which correlated well with conventional venom extract-specific IgE detection (r=0.762 and r=0.757, respectively). In contrast, the PPV of rApi m 1-specific IgE detection at the time of diagnosis was 34.8%. Three years of venom immunotherapy resulted in decreased venom-specific IgE, particularly IgE specific for Vespidae venom components. Stings by yellow jackets and male sex may be risk factors for hymenoptera venom allergy in Korea. Vespidae component-specific IgE, but not Apidae component-specific IgE, had diagnostic and monitoring value in hymenoptera venom allergy comparable to that of conventional hymenoptera venom extract-specific IgE.Allergy, asthma & immunology research 09/2012; 4(5):284-9. · 1.91 Impact Factor -
Article: Profiling the proteome of the venom from the social wasp Polybia paulista: a clue to understand the envenoming mechanism.
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ABSTRACT: The study reported here is a classical bottom-up proteomic approach where proteins from wasp venom were extracted and separated by 2-DE; the individual protein spots were proteolytically digested and subsequently identified by using tandem mass spectrometry and database query with the protein search engine MASCOT. Eighty-four venom proteins belonging to 12 different molecular functions were identified. These proteins were classified into three groups; the first is constituted of typical venom proteins: antigens-5, hyaluronidases, phospholipases, heat shock proteins, metalloproteinases, metalloproteinase-desintegrin like proteins, serine proteinases, proteinase inhibitors, vascular endothelial growth factor-related protein, arginine kinases, Sol i-II and -II like proteins, alpha-glucosidase, and superoxide dismutases. The second contained proteins structurally related to the muscles that involves the venom reservoir. The third group, associated with the housekeeping of cells from venom glands, was composed of enzymes, membrane proteins of different types, and transcriptional factors. The composition of P. paulista venom permits us to hypothesize about a general envenoming mechanism based on five actions: (i) diffusion of venom through the tissues and to the blood, (ii) tissue, (iii) hemolysis, (iv) inflammation, and (v) allergy-played by antigen-5, PLA1, hyaluronidase, HSP 60, HSP 90, and arginine kinases.Journal of Proteome Research 08/2010; 9(8):3867-77. · 5.11 Impact Factor
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Keywords
'CCD negative' patients
'CCD positive'
'CCD positive' patients
259 HV allergic patients
anti-CCD sIgE
CAP tests
carbohydrate determinants
clinical reactivity
DV allergy
DV skin test positivity
HV allergic patients
multivalent pollen sensitization
mutual sIgE inhibition tests
pollen CAP tests
pollen sensitization
positive CAP tests
Skin prick tests
sting induced anti-CCD sIgE
sting induced anti-pollen sIgE
venom glycoproteins