Latin name: Yellow Jacket
Family: Vespula vulgaris
Common names: phospholipase A1, PLA1
Ves v 1
Ves v 1 (1). rVes v 1 is a CCD-free recombinant protein.
Approximately 37 kDa.
Other allergens isolated
Allergens characterised to date include:
- Ves v 1, a phospholipase. (1, 2, 3, 4, 5, 6, 7)
- Ves v 2, a 43 kDa protein, a hyaluronidase. (2, 3, 4, 5, 8, 9, 10, 11)
- Ves v 3, a dipeptidyl-peptidase. (2, 12, 13)
- Ves v 5, a 100-105 kDa protein, also known as antigen 5 or Ag5. (2, 3, 4, 5, 10, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23)
Ves v 1, also known phospholipase A1, PLA1, is a 37 kDa protein. It is a phospholipase. Ves v 1 is one of three major allergens found in Yellow Jacket venom: Ves v 1 (phospholipase A1), Ves v 2 (hyaluronidase), and Ves v 5 (antigen 5). (21)
However, in addition to the presence of allergens, Hymenoptera venoms are rich sources of biologically active compounds which contain a complex mixture of amines, small peptides and high-molecular-weight proteins such as enzymes and toxins. (24) These other compounds may be relevant; for example, local reactions may result from biologically active peptides and polycationic peptides such as bradykinin-like peptides, chemotactic peptides and other components such as neurotoxic kinins and mastoparans. (24, 25, 26, 27)
Ves v 1, a 37 kDa protein, a phospholipase, is a triglyceride lipase. These are lipolytic enzymes that hydrolyse ester linkages of triglycerides. (28) Lipases are widely distributed in animals, plants and prokaryotes. Ves v 1, a phospholipase A1 (PLA1), comprises the whole of group 1 of vespid and ant venom allergens. These have no sequence similarity with bee venom phospholipase A2. (29, 30)
The Vespidae family includes hornets (genera Vespa and Dolichovespula), yellow jackets (genus Vespula) and the paper wasp (genus Polistes).
Vespid phospholipases are homologous to porcine pancreatic lipase, among others (Table 1).(29)
Table 1: Examples of Phospholipase A1 have been isolated from various vespid and ant species.
Dol m 1
Dolichovespula maculate (bald-faced hornet)
Pol a 1
Polistes annularis (paper wasp)
Pol d 1
Polistes dominulus (European paper wasp)
Poly p 1
Polybia paulista (neotropical social wasp)
Pro ca 38kD
Protortonia cacti (cochineal)
Sol i 1
Solenopsis invicta (red fire ant)
Sus s Lipase
Sus scrofa domestica (domestic pig)
Ves g 1
Vespula germanica (German yellow jacket)
Ves m 1
Vespula maculifrons (Eastern yellow jacket)
Ves v 1
Vespula vulgaris (yellow jacket)
Ves c 1
Vespa crabo (European hornet)
As most vespid-allergic patients show multiple reactions to more than one vespid venom, (39, 40) partial antigenic identity of the component proteins is suggested, (24) i.e. patients show a varying extent of cross-reactivity to related panallergens, e.g. Antigen 5's. (21)
Bees, fire ants and vespids each have unique as well as homologous venom allergens: one of the four known bee allergens is homologous to vespid hyaluronidases, with about 50% sequence identity. Two of the four known fire ant allergens are homologous to vespid antigen 5 and phospholipases.
There is greater cross-reactivity between hornet and yellow jacket allergens than that between hornet (or yellow jacket) and wasp allergens. The order of cross-reaction of the three vespid allergens are hyaluronidase > antigen 5 > phospholipase. (4)
Hymenoptera venom allergy is usually an IgE-mediated allergic hypersensitivity of non-atopic origin. (41) The most frequent clinical patterns are: (i) large local reactions exceeding 10 cm in diameter and 24 hours in duration and (ii) rapid-onset (usually within 10 minutes after sting) generalised immediate-type hypersensitivity reactions such as pruritus, urticaria, angioedema, nausea, vomiting, diarrhoea, rhinoconjunctivitis, bronchospasm, hypotension, cardiovascular collapse and unconsciousness. (42, 43, 44, 45) Systemic reactions have been reported to occur in 0.8 to 5% of the general population. (46) These are mostly IgE-mediated and may be severe and even life-threatening, with 0.09 to 0.45 deaths per million within the general population. (47, 48)
Large doses of venom may result in unusual reactions such as haemolysis, coagulopathy, rhabdomyolysis, acute renal failure and hepatotoxicity. Aortic thrombosis and cerebral infarction has also been reported as a clinical symptom after massive wasp stings. (24, 42, 49, 50)
It is clear that knowledge of the composition of venoms and structure of allergens is a prerequisite for the accurate diagnosis and treatment of insect venom allergy. (51)
See Yellow Jacket i3 for clinical information and further details on Yellow Jacket allergy.
Estimates of the worldwide annual incidence of immunologic reactions to hymenopteran stings in the world population range from 0.3% to 3.0%, or nearly 100 million cases per year, ranging from local wheal-and-flare reactions to deaths from anaphylactic shock. In the United States, the annual incidence of allergic reactions to hymenopteran stings ranges between 0.4% and 4.0%, with 40 to 50 deaths a year. (52) Hymenoptera include the apids (bumblebee, honeybee, carpenter bee), vespids (hornets, wasps, yellow jackets), and formicids (fire ants, bulldog ants, bullet ants, etc.).
Skin tests and assessment of serum-specific IgE antibodies are used to diagnose venom allergy. Although determination of specific-serum IgE antibodies to Hymenoptera venoms is a very sensitive diagnostic test for venom allergy, unfortunately the test lacks absolute sensitivity and specificity. (53) Possible reasons for the inaccuracy of diagnostic tests with Hymenoptera venom (which may increase or decrease in sensitivity since last sting) (54, 55) include wide variability of venom amount applied with one sting, especially in vespids. (56, 57)
Less than 5% of history-positive individuals are negative in both skin and serum IgE if investigated within a year after a systemic reaction to Hymenoptera stings. Furthermore, up to 20% of individuals with no history of adverse reactions to Hymenoptera stings may react positively to either or both tests. (58) Test-positive individuals will develop a systemic reaction more frequently than test-negative individuals when re-stung; however, only some of the test-positive patients will react again. Additionally, some test-negative individuals may develop systemic reactions. (58, 59, 60)
The three allergens thought to be primarily responsible for IgE-mediated allergic reactions to yellow jacket are phospholipase A1 (Ves v 1), hyaluronidase (Ves v 2), and antigen 5 (Ves v 5). (5, 61, 62) Both Ves v 2 and Ves v 3 are glycoproteins prone to CCD reactivity with homologous allergens in honey bee venom. By contrast, Ves v 1 and Ves v 5 are non-glycosylated, and unique candidates for the diagnosis of yellow jacket venom allergy. (1)
Recombinant allergens may aid in the diagnosis of patients who have negative specific IgE responses to insect venom despite a history of severe clinical reactivity and a positive skin-test response. For example, an evaluation of the major allergens with either high abundance (e.g. honey bee Api m 1; yellow jacket Ves v 5) or low abundance (e.g. honey bee Api m 3; Api m 2) in patients receiving specific immunotherapy (SIT) with either honey bee (n=20) or vespid (n=22) venom extracts found that of the 8 patients who had been non-reactive to bee venom in classical serum IgE tests using whole venom extract (group A), no or rare serum IgE was found with the abundant major allergen Api m 1 (0/8) or the less abundant major allergen Api m 2 (2/8).
Among the vespid venom-allergic patients, none showed serum IgE to the major vespid venom allergens Ves v 1, Ves v 2, or Ves v 5 in immunoblots, whereas one patient had demonstrable serum IgE against rVes v 5 (1/22). Therefore, due to the known low relative abundance of Api m 3 in native honey bee venom, rApi m 3 was a valuable tool in the diagnosis of honey bee venom allergy. The authors concluded that it was likely that diagnostic failures in vespid venom allergy are caused by serum-IgE reactivity against hitherto unidentified allergens in native vespid venom. (63)
Among patients with allergy to insect stings, double positivity in tests for IgE antibodies specific to honey bee and wasp (Vespula) venoms is a frequent diagnostic problem, and in particular makes selection of venom for immunotherapy problematic. Up to 50% of patients with allergic reactions to honey bee or Vespula stings are double-positive to both, i.e. they also have specific IgE to the other venom. (51, 64) This may be explained by true double sensitisation to both if the patient was stung by both honey bees and wasps, or by cross-reactivity between allergens of the two venoms, e.g. hyaluronidase and/or dipeptidylpeptidases, or between the carbohydrate epitopes (cross-reacting carbohydrate determinants (CCDs)) they share. (12, 64, 65, 66)
The relevance of CCDs in protein-directed cross-reactivity is controversial; whereas in Hymenoptera allergy it is thought to be clinically irrelevant, but diagnostically problematic. (1, 67, 68)
For example, a study examined the frequency of sensitisation to CCDs and their role in double positivity in a group of 100 patients allergic to vespula or honey bee stings and skin-prick test-positive to the respective venom. Serum IgE to bee venom, vespula venom and cross-reacting carbohydrate determinants (CCDs), and serum IgE to species-specific recombinant major allergens Api m1 (honey bee) and Ves v5 (Vespula) were assessed. Double positivity was observed in 59% of allergic patients. Serum lgE to Api m1 was detected in 97% of honey bee- and 17% of vespula-allergic patients. Serum lgE to Ves v 5 was demonstrated in 87% of Vespula- and 17% of honey bee-allergic patients. CCD serum IgE was present in 37% of all allergic patients and in 56% of those with double positivity, and was more frequent in bee venom- than in Vespula venom-allergic patients.
The authors concluded that double positivity of IgE to honey bee and Vespula venom was often caused by cross-reactions, particularly to CCDs, and that serum IgE to both Api m1 and Ves v5 indicates that true double sensitisation and immunotherapy with both venoms will be required. (64) Other researchers have reported similar findings. (69)
Honey bee venom phospholipase A2 and hyaluronidase are different from the Vespula enzymes, so there is little significant cross-reactivity. (70)
Therefore: as double positivity of IgE to honey bee and Vespula venom is often caused by cross-reactions, especially with CCDs, utilising a specific marker allergen may be of use to discern the difference. (64)
Such double positivity causes significant problems, including in the selection of venoms for immunotherapy: if double sensitisation is true for both venoms, this would indicate potential systemic allergic reactions to sting by both insect species, and immunotherapy with both venoms would be required. Species-specific recombinant major allergens may reduce the need for expensive inhibition tests required to demonstrate this, and would thus steer the choice of venoms for immunotherapy. (64)
In this instance, recombinant Ves v 1 (rVes v 1) may play a diagnostic role. In a study evaluating rVes v 1, of 20 double-positive patient sera, 15 showed reactivity to rVes v 1, 10 of which additionally had specific IgE to rVes v 5. Only 1 out of these 20 sera had serum IgE raised to rVes v 5 exclusively, while 2 sera exhibited additional reactivity to Api m 1. An overall diagnostic sensitivity of 80% could be achieved by use of two yellow jacket-venom allergens, compared to 50% when using rVes v 5 solely.
Of the remaining 4 patients, 2 had serum IgE to Api m 1 and 1 was reactive to the CCD marker MUXF-BSA only. Therefore, for 16 of the 20 patients (80%), a particular culprit venom could convincingly be assigned, whereas 2 patients showed a true double sensitisation. Only 1 patient showed no reactivity to either Ves v 1 or to Ves v 5. (This patient also showed no reactivity to other vespid proteins such as the hyluronidases Ves v 2a and b, or the dipeptidylpeptidase Ves v 3.)
In the yellow jacket-venom mono-sensitised group, 11 of 14 sera (79%) were reactive to rVes v 1, 7 of which exhibited additional serum IgE reactivity to rVes v 5. Two further patients showed serum IgE reactivity exclusively to rVes v 5. In summary, 13 of 14 (93%) had detectable serum IgE either to rVes v 1 or rVes v 5 or both, while 1 patient with low total yellow jacket-venom sIgE showed no reactivity. (1)
These data demonstrate that recombinant Ves v 1 is a necessity for assessing the sensitisation of individuals to yellow jacket venom, and its recombinant availability (complemented by Ves v 5 and Api m 1) allows for clear assignment of sensitisation patterns. (1)
Component Resolved Diagnosis (CRD) using recombinant allergens may be useful in various other scenarios. Only 30 to 50% of those with positive IgE tests will react to a subsequent sting by the same insect. (71) Sting-provocation tests during venom immunotherapy have shown that approximately 95% of patients allergic to vespid stings and 80-90% of those allergic to honey bee venom are completely protected from developing generalised allergic symptoms. (57, 71) CRD may be able to identify these individuals.
Furthermore, systemic allergic side-effects to immunotherapy injections may occur in 20 to 40% of patients during immunotherapy with honey bee venom, and 5 to 10% during immunotherapy with vespid venoms. (57) As a result of the recombinant venom allergens available today, and others in development, there is considerable potential for improvement of both diagnosis and immunotherapy of Hymenoptera-venom allergy. (72)
Diagnostic methods, e.g. skin- and serum-specific IgE, are based on natural yellow jacket extracts that contain both allergenic and non-allergenic proteins, and may contain major allergens in insufficient concentrations, or may be contaminated with unwanted components to which the patients are not allergic. Furthermore, important allergens may be lost during extraction because of (among other things) the activity of proteases co-purified with the allergens, or the protease nature of some of the allergens. (75)
A great variability and difficulty in standardisation exists because the extract composition depends on the origin of the raw material, and on the extraction, purification and storage procedures. (73) Recombinant allergens lead to standardised reagents that are biochemically characterised, and therefore to results that are comparable. Furthermore, recombinant allergens produced in E. coli lack carbohydrate determinants (CCDs), thereby eliminating the risk of false-positive results. (74)
The advantages of recombinant allergens include unlimited availability in their identical form, which allows for optimal standardisation; and the absence of contamination by traces of other allergens which might confound the true relevance of an individual allergen for the respective allergic disease. (75) Given also that the potency of natural allergens varies, (76) utilising recombinant allergens may allow more precise measurement and evaluation of IgE responses in certain instances, in particular for more appropriate diagnoses when used in Component Resolved Diagnosis (CRD), for exploring cross-reactivity, and for immunotherapy. (77)
Importantly, patients are not always able to provide the entomologic identification of the culprit responsible for a severe anaphylactic episode, precluding institution of the required life-saving venom-specific immunotherapy, and recombinant single allergens may be of benefit in such cases.
Therefore, as yellow jacket venom contains two non-glycosylated major allergens without significant cross-reactive homologues in other species, Ves v 1 and Ves v 5, and which have high IgE prevalence, (78) use of recombinant Ves v 1 and Ves v 5 provides a significant improvement in identification of the culprit venom, which is essential for choosing the appropriate immunotherapeutic strategy. Furthermore, recombinant Ves v 1 for routine diagnosis enables improved assessment of its true IgE prevalence and clinical relevance.
Compiled by Dr Harris Steinman, developer of Allergy Advisor, firstname.lastname@example.org
- Seismann H, Blank S, Cifuentes L, Braren I, Bredehorst R, Grunwald T, Ollert M, Spillner E. Recombinant phospholipase A1 (Ves v 1) from yellow jacket venom for improved diagnosis of hymenoptera venom hypersensitivity. Clin Mol Allergy 2010;8(1):7.
- International Union of Immunological Societies Allergen Nomenclature: IUIS official list http://www.allergen.org/ 2011.
- King TP, Guralnick M. Hymenoptera allergens. Clin Allergy Immunol 2004;18:339-53.
- King TP, Lu G, Gonzalez M, Qian N, Soldatova L. Yellow jacket venom allergens, hyaluronidase and phospholipase: sequence similarity and antigenic cross-reactivity with their hornet and wasp homologs and possible implications for clinical allergy. J Allergy Clin Immunol 1996;98(3):588-600.
- King TP, Alagon AC, Kuan J, Sobotka AK, Lichtenstein LM. Immunochemical studies of yellowjacket venom proteins. Mol Immunol 1983;20(3):297-308.
- Meriney D, Goel Z, Grieco MH. Allergens in yellow jacket venom as determined by sephadex fractionation, enzyme and RAST assays. J Clin Lab Immunol 1981;5(1):1-5.
- Hoffman DR. Allergens in hymenoptera venom. V. Identification of some of the enzymes and demonstration of multiple allergens in yellow jacket venom. Ann Allergy 1978;40(3):171-6.
- Jin C, Focke M, Leonard R, Jarisch R, Altmann F, Hemmer W. Reassessing the role of hyaluronidase in yellow jacket venom allergy. J Allergy Clin Immunol 2010;125(1):184-190.e1.
- Seppälä U, Selby D, Monsalve R, King TP, Ebner C, Roepstorff P, Bohle B. Structural and immunological characterization of the N-glycans from the major yellow jacket allergen Ves v 2: the N-glycan structures are needed for the human antibody recognition. Mol Immunol 2009;46(10):2014-21.
- Kolarich D, Loos A, Léonard R, Mach L, Marzban G, Hemmer W, Altmann F. A proteomic study of the major allergens from yellow jacket venoms. Proteomics 2007;7(10):1615-23.
- Kolarich D, Leonard R, Hemmer W, Altmann F. The N-glycans of yellow jacket venom hyaluronidases and the protein sequence of its major isoform in Vespula vulgaris. FEBS J 2005;272(20):5182-90.
- De Graaf DC, Aerts M, Danneels E, Devreese B. Bee, wasp and ant venomics pave the way for a component-resolved diagnosis of sting allergy. J Proteomics 2009;72(2):145-54.
- Wypych JI, Abeyounis CJ, Reisman RE. Analysis of differing patterns of cross-reactivity of honeybee and yellow jacket venom-specific IgE: use of purified venom fractions. Int Arch Allergy Appl Immunol 1989;89(1):60-6.
- Bohle B, Zwolfer B, Fischer GF, Seppala U, Kinaciyan T, Bolwig C, Spangfort MD, Ebner C. Characterization of the human T cell response to antigen 5 from Vespula vulgaris (Ves v 5). Clin Exp Allergy 2005;35(3):367-73.
- Winkler B, Bolwig C, Seppala U, Spangfort MD, Ebner C, Wiedermann U. Allergen-specific immunosuppression by mucosal treatment with recombinant Ves v 5, a major allergen of Vespula vulgaris venom, in a murine model of wasp venom allergy. Immunology 2003;110(3):376-85.
- King TP, Jim SY, Monsalve RI, Kagey-Sobotka A, Lichtenstein LM, Spangfort MD. Recombinant allergens with reduced allergenicity but retaining immunogenicity of the natural allergens: hybrids of yellow jacket and paper wasp venom allergen antigen 5s. J Immunol 2001;166(10):6057-65.
- Suck R, Weber B, Kahlert H, Hagen S, Cromwell O, Fiebig H. Purification and immunobiochemical characterization of folding variants of the recombinant major wasp allergen Ves v 5 (antigen 5). Int Arch Allergy Immunol 2000;121(4):284-91.
- Monsalve RI, Lu G, King TP. Expression of yellow jacket and wasp venom Ag5 allergens in bacteria and in yeast. Arb Paul Ehrlich Inst Bundesamt Sera Impfstoffe Frankf A M. 1999;(93):181-8.
- Monsalve RI, Lu G, King TP. Expressions of recombinant venom allergen, antigen 5 of yellowjacket (Vespula vulgaris) and paper wasp (Polistes annularis), in bacteria or yeast. Protein Expr Purif 1999;16(3):410-6.
- Kischnick S, Weber B, Verdino P, Keller W, Sanders EA, Anspach FB, Fiebig H, Cromwell O, Suck R. Bacterial fermentation of recombinant major wasp allergen Antigen 5 using oxygen limiting growth conditions improves yield and quality of inclusion bodies. Protein Expr Purif 2006;47(2):621-8.
- Henriksen A, King TP, Mirza O, Monsalve RI, Meno K, Ipsen H, Larsen JN, Gajhede M, Spangfort MD. Major venom allergen of yellow jackets, Ves v 5: structural characterization of a pathogenesis-related protein superfamily. Proteins 2001;45(4):438-48.
- Lu G, Villalba M, Coscia MR, Hoffman DR, King TP. Sequence analysis and antigenic cross-reactivity of a venom allergen, antigen 5, from hornets, wasps, and yellow jackets. J Immunol 1993;150(7):2823-30.
- King TP, Kochoumian L, Lam T. Immunochemical observations of antigen 5, a major venom allergen of hornets, yellowjackets and wasps. Mol Immunol 1987;24(8):857-64.
- Monteiro MC, Romão PR, Soares AM. Pharmacological perspectives of wasp venom. Protein Pept Lett 2009;16(8):944-52.
- Habermann, E. Bee and wasp venoms. Science 1972;177:314-22.
- Nakajima T. Biochemistry of vespid venoms. In: Tu AT (Ed). Handbook of Natural Toxins. Marcel Dekker, New York. 1984;(2):109-33.
- Piek T. Pharmacology of hymenoptera venom. In: Tu AT (Ed). Handbook of Natural Toxins. Marcel Dekker, New York. 1984;(2):135-85.
- AllFam Database of allergen families. AF037: Lipase. http://www.meduniwien.ac.at/allergens/allfam/factsheet.php?allfam_id=AF037. Accessed 15 April 2011.
- Nair BC, Nair C, Denne S, Wypych J, Arbesman CE, Elliott WB. Immunologic comparison of phospholipases A present in Hymenoptera insect venoms. J Allergy Clin Immunol 1976;58(1 PT 1):101-9.
- King TP, Spangfort MD. Structure and biology of stinging insect venom allergens. Int Arch Allergy Immunol. 2000;123(2):99-106.
- Soldatova L, Kochoumian L, King TP. Sequence similarity of a hornet (D. maculata) venom allergen phospholipase A1 with mammalian lipases. FEBS Lett 1993;320:145-9.
- Moawad TI, Hoffman DR, Zalat S. Isolation, cloning and characterization of Polistes dominulus venom phospholipase A1 and its isoforms. Acta Biol Hung. 2005;56(3):261-74.
- Santos LD, Santos KS, de Souza BM, Arcuri HA, Cunha-Neto E, Castro FM, Kalil JE, Palma MS. Purification, sequencing and structural characterization of the phospholipase A(1) from the venom of the social wasp Polybia paulista (Hymenoptera, Vespidae). Toxicon 2007;50(7):923-37.
- Ohgiya Y, Arakawa F, Akiyama H, Yoshioka Y, Hayashi Y, Sakai S, Ito S, Yamakawa Y, Ohgiya S, Ikezawa Z, Teshima R. Molecular cloning, expression, and characterization of a major 38-kd cochineal allergen. J Allergy Clin Immunol 2009;123(5):1157-62, 1162.e1-4.
- Hoffman DR. Allergens in Hymenoptera venom XXIV: the amino acid sequences of imported fire ant venom allergens Sol i II, Sol i III, and Sol i IV. J Allergy Clin Immunol 1993;91(1 Pt 1):71-8.
- Park HS, Kim HY, Suh YJ, Lee SJ, Lee SK, Kim SS, Nahm DH. Alpha amylase is a major allergenic component in occupational asthma patients caused by porcine pancreatic extract. J Asthma 2002;39(6):511-6.
- Hoffman DR, Wood CL. Allergens in Hymenoptera venom XI. Isolation of protein allergens from Vespula maculifrons (yellow jacket) venom. J Allergy Clin Immunol 1984;74(1):93-103.
- Hoffman DR. Allergens in Hymenoptera venom. XXV: The amino acid sequences of antigen 5 molecules and the structural basis of antigenic cross-reactivity. J Allergy Clin Immunol 1993;92(5):707-16.
- Lichtenstein LM, Valentine MD, Sobotka AK. Insect allergy: the state of the art. J Allergy Clin Immunol 1979;64(1):5-12.
- King TP, Joslyn A, Kochoumian L. Antigenic cross-reactivity of venom proteins from hornets, wasps, and yellow jackets. J Allergy Clin Immunol 1985;75(5):621-8.
- Johansson SG, Hourihane JO, Bousquet J, Bruijnzeel-Koomen C, Dreborg S, Haahtela T, et al. A revised nomenclature for allergy. An EAAC1 position statement from the EAACI nomenclature task force. Allergy 2001;56:813-24.
- Müller UR. Insect sting allergy clinical picture, diagnosis, and treatment. Oustav Fischer Verlag, Ed.; Stuttgart-New York, 1990.
- Vachvanichsanong P, Dissaneewate P, Mitarnun W. Non-fatal acute renal failure due to wasp stings in children. Pediatr Nephrol 1997;11(6):734-6.
- Daher Ede F, da Silva Júnior GB, Bezerra GP, Pontes LB, Martins AM, Guimarães JA. Acute renal failure after massive honeybee stings. Rev Inst Med Trop Sao Paulo 2003;45(1):45-50.
- Ebo DG, Hagendorens MM, Stevens WJ. Hymenoptera venom allergy. Expert Rev Clin Immunol 2005;1:169-75.
- Charpin D, Birnbaum J, Lanteaume A, Vervloet D. Prevalence of allergy to hymenoptera stings in different samples of the general population. J Allergy Clin Immunol 1992;90(3 Pt 1):331-4.
- Mosbech H. Deaths resulting from bee and wasp stings in Denmark 1960-1980. [Danish] Ugeskr Laeger 1983;145(23):1757-60.
- Müller U. Epidemiology of insect sting allergy. In: Burr ML (Ed). Epidemiology of clinical allergy. Monogr Allergy 1993;31:131-46.
- De Bandt M, Atassi-Dumont M, Kahn MF, Herman D. Serum sickness after wasp venom immunotherapy: clinical and biological study. J Rheumatol 1997;24(6):1195-7.
- Boz C, Velioglu S, Ozmenoglu M. Acute disseminated encephalomyelitis after bee sting. Neurol Sci 2003;23(6):313-5.
- Bilo BM, Rueff F, Mosbech H, Bonifazi F, Oude-Elberink JN. Diagnosis of Hymenoptera venom allergy. Allergy 2005;60(11):1339-49.
- Diaz JH. Recognition, management, and prevention of hymenopteran stings and allergic reactions in travelers. J Travel Med 2009;16(5):357-64.
- Guerti K, Bridts CH, Stevens WJ, Ebo DG. Wasp venom-specific IgE: towards a new decision threshold? J Investig Allergol Clin Immunol 2008;18(4):321-3.
- Müller U, Fricker M, Wymann D, Blaser K, Crameri R. Increased specificity of diagnostic tests with recombinant major bee venom allergen phospholipase A2. Clin Exp Allergy 1997;27(8):915-20.
- Müller U. Insect sting allergy: Clinical picture, diagnosis and treatment. Stuttgart, New York: Gustav Fischer Verlag, 1990.
- Hoffman DR, Jacobson RS. Allergens in hymenoptera venom XII: how much protein is in a sting? Ann Allergy 1984;52(4):276-8.
- Müller U, Helbling A, Berchtold E. Immunotherapy with honeybee venom and yellow jacket venom is different regarding efficacy and safety. J Allergy Clin Immunol 1992;89(2):529-35.
- Müller U. Diagnosis and management of hymenoptera venom allergy. In: Bousquet J, Michel FB (Eds). Advances in Allergology and Clinical Immunology, Paris 1992, The Parthenon Publishing Group:611-22.
- Blaauw PJ, Smithuis LO. The evaluation of the common diagnostic methods of hypersensitivity for bee and yellow jacket venom by means of an in-hospital insect sting. J Allergy Clin Immunol 1985;75(5):556-62.
- Van der Linden PW, Hack CE, Struyvenberg A, Van der Zwan JK. Insect-sting challenge in 324 subjects with a previous anaphylactic reaction: current criteria for insect-venom hypersensitivity do not predict the occurrence and the severity of anaphylaxis. J Allergy Clin Immunol 1994;94(2 Pt 1):151-9.
- Seismann H, Blank S, Braren I, Greunke K, Cifuentes L, Grunwald T, Bredehorst R, Ollert M, Spillner E. Dissecting cross-reactivity in hymenoptera venom allergy by circumvention of alpha-1,3-core fucosylation. Mol Immunol 2010;47(4):799-808.
- Blank S, Seismann H, Bockisch B, Braren I, Cifuentes L, McIntyre M, Rühl D, Ring J, Bredehorst R, Ollert MW, Grunwald T, Spillner E. Identification, recombinant expression, and characterization of the 100 kDa high molecular weight Hymenoptera venom allergens Api m 5 and Ves v 3. J Immunol 2010;184(9):5403-13.
- Cifuentes LB, Blank S, Vosseler S, Grunwald T, Mempel M, Darsow U, Ring J, Bredehorst R, Spillner E, Ollert M. Insect venom allergy with negative venom-specific IgE: the use of recombinant allergens provides an improved diagnostic solution. (Poster) 2nd Int Symp Molecular Allergol, Rome, Italy 2007;April 22-24.
- Muller UR, Johansen N, Petersen AB, Fromberg-Nielsen J, Haeberli G. Hymenoptera venom allergy: analysis of double positivity to honey bee and Vespula venom by estimation of IgE antibodies to species-specific major allergens Api m1 and Ves v5. Allergy 2009;64(4):543-8.
- Hemmer W, Focke M, Kolarich D, Wilson IB, Altmann F, Wöhrl S, Götz M, Jarisch R. Antibody binding to venom carbohydrates is a frequent cause for double positivity to honeybee and yellow jacket venom in patients with stinging-insect allergy. J Allergy Clin Immunol 2001;108(6):1045-52.
- Hemmer W. Cross-reactivity to honeybee and wasp venom. [German] Hautarzt 2008;59(3):194-9.
- Kochuyt AM, Van Hoeyveld EM, Stevens EA. 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. Clin Exp Allergy 2005;35(4):441-7.
- Mari A. IgE to cross-reactive carbohydrate determinants: analysis of the distribution and appraisal of the in vivo and in vitro reactivity. Int Arch Allergy Immunol 2002;129(4):286-95.
- Erzen R, Korosec P, Silar M, Music E, Kosnik M. Carbohydrate epitopes as a cause of cross-reactivity in patients allergic to Hymenopter. [German] Wien Klin Wochenschr 2009;121(9-10):349-52.
- Weber RW. On the cover: Honeybees. Ann Allergy Asthma Immunol 2005;95(1):1-6.
- Ruëff F, Przybilla B, Müller U, Mosbech H. The sting challenge test in Hymenoptera venom allergy. Position paper of the Subcommittee on Insect Venom Allergy of the European Academy of Allergology and Clinical Immunology. Allergy 1996;51(4):216-25.
- Müller UR. Recombinant Hymenoptera venom allergens. Allergy 2002;57(7):570-6.
- Hefle SL, Helm RM, Burks AW, Bush RK. Comparison of commercial peanut skin test extracts. J Allergy Clin Immunol 1995;95(4):837-42.
- Van Ree R. Carbohydrate epitopes and their relevance for the diagnosis and treatment of allergic diseases. Int Arch Allergy Immunol 2002;129(3):189-97.
- Scheiner O, Kraft D. Basic and practical aspects of recombinant allergens. Allergy 1995;50(5):384-91.
- Peeters KA, Koppelman SJ, Van Hoffen E, Van der Tas CW, Den Hartog Jager CF, Penninks AH, Hefle SL, Bruijnzeel-Koomen CA, Knol EF, Knulst AC. Does skin prick test reactivity to purified allergens correlate with clinical severity of peanut allergy? Clin Exp Allergy 2007;37(1):108-15.
- Kazemi-Shirazi L, Niederberger V, Linhart B, Lidholm J, Kraft D, Valenta R. Recombinant marker allergens: diagnostic gatekeepers for the treatment of allergy. Int Arch Allergy Immunol 2002;127(4):259-68.
- Binder M, Fierlbeck G, King T, Valent P, Bühring HJ. Individual hymenoptera venom compounds induce upregulation of the basophil activation marker ectonucleotide pyrophosphatase/phosphodiesterase 3 (CD203c) in sensitized patients. Int Arch Allergy Immunol 2002;129(2):160-8.