Honey bee

Further reading

Phospholipase A2 k203

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Code: i1
Latin name: Apis mellifera
Source material: Venom
Family: Apidae
Order: Hymenoptera
 
Honeybee is the only stinging Hymenoptera that nearly always leaves its fluked stinger in the skin of the victim.

Allergen Exposure

The natural range of the honeybee is thought to be Africa, Europe and the Middle East for A. mellifera and Japan, India and Indochina for A. cerona. Honeybees have been domesticated and spread throughout the world. Honeybee is the only stinging Hymenoptera that almost always leaves its fluked stinger in the skin of the victim. The venom continues to pump into the victim until the venom sac is exhausted or the stinger removed.

Potential Cross-Reactivity

Venoms from honeybees and bumblebees are reported to be highly cross-reactive, which is consistent with the degree of structural similarity in the phospholipases, phospholipase A2 (1, 2, 3). The hyaluronidases and phosphatases also have a high degree of similarity in honeybees and bumblebees (1, 2, 3, 4).
The antigenic cross-reactivity between honeybee and Vespula venom is limited and largely confined to hyaluronidase (5, 6, 7, 8). Bee venom hyaluronidase has a 55% sequence identity with vespid hyaluronidase (4).

Clinical Experience

Studies indicate that a large percentage of the general population (15-25%) can be sensitized to Hymentoptera venoms. In rural populations the frequency may be even higher indicating that the prevalence of specific IgE antibodies is related to the degree of exposure to the Hymenoptera. Systemic reactions occur in 0,15-5% of the general population and may occasionally be fatal (9, 10).

Since the risk of bee sting allergy increases with the degree of exposure, beekeepers are at a high risk for bee sting allergy (11).
 
Review
The natural range of the honeybee is thought to be Africa, Europe and the Middle East for A. mellifera and Japan, India and Indo China for A. cerona. Honeybees have been domesticated and spread throughout the world.

Honeybee is the only stinging Hymenoptera that almost always leaves its fluked stinger in the skin of the victim. The venom continues to pump into the victim until the venom sac is exhausted or the stinger removed.
 
Venoms from honeybees and bumblebees are reported to be highly cross-reactive, which is consistent with the degree of structural similarity in the phospholipases, phospholipase A2 (1, 2, 3). The hyaluronidases and phosphatases also have a high degree of similarity in honeybees and bumblebees (1, 2, 3, 4).

The antigenic cross-reactivity between honeybee and Vespula venom is limited and largely confined to hyaluronidase (5, 6, 7, 8). Bee venom hyaluronidase has a 55% sequence identity with vespid hyaluronidase (4).
 
Studies indicate that a large percentage of the general population (15-25%) can be sensitized to Hymentoptera venoms. In rural populations the frequency may be even higher indicating that the degree of exposure is related to the prevalence of specific IgE antibodies to the Hymenoptera. Systemic reactions occur in 0,15-5% of the general population and may occasionally be fatal (9, 10).

Since the risk of bee sting allergy increases with the degree of exposure, beekeepers are at a high risk for bee sting allergy (11).
 
Bee venom is a complex mixture of peptides and glucoproteins, most of which are enzymes (12). Most insect venom allergens have a molecular weight of 10-50 kD with the exception of the bee venom peptide melittin (4, 13). Studies also report IgE and T-cell response to high-molecular weight allergens (12, 14).

Major allergens include phospholipase A (PLA2), hyaluronidase acid and phosphatase (4, 12, 15, 16, 17, 18). Melittin is one of the smallest molecules known to be an allergen, with only 26 amino acid residues that associate in solution to form a tetramer of about 11 kD (5, 13).
 
Allergens
Common name                   Allergen name             Molecular size, kD
 
Phospholipase A2                  Api m1                                 16
 
Hyaluronidase                       Api m2                                 39
 
Acid phosphatase                  Api m3                                 43
 
Melittin                                 Api m4                                   3

References

  1. Hoffman DR, Jacobson RS. Allergens in Hymenoptera venom XXVII: Bumblebee venom allergy and allergens. J Allergy Clin Immunol 1996;97:812-21. 
  2. Stapel SO, Waanders-Lijster de Raadt J, van Toorenenbergen AW, de Groot H. Allergy to bumblebee venom. II. IgE cross-reactivity between bumblebee and honeybee venom. Allergy 1998;53:769-77.
  3. Annila I. Bee venom allergy. Clin Exp Allergy 2000;30:1682-87.
  4. King TP, Spangfort MD. Structure and Biology of Stinging Insect Venom Allergens. Int Arch Allergy Immunol 2000;123:99-106.
  5. Sobotka AK, Adkinson NF, Valentine MD, Lichtenstein LM. Allergy to insect stings. IV. Diagnosis by Radioallergosorbent test (R.A.S.T.). J Immunol 1978;121: 2477-84.
  6. 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;89:60-6.
  7. Castro FFM, Palma MS, Brochetto-Braga MR, Malaspina O, Lazaretti J, Baldo MAB et al. Biochemical properties and study of antigenic cross-reactivity between Africanized honey bee and wasp venom. J Invest Allergol Clin Immunol 1994;4:37-41.
  8. Hoffman DR, Dove, De, Moffitt JE, Stafford CT. Allergens in Hymenoptera venom XII. Cross-reativity and multiple reactivity between fire ant venom, bee and wasp venoms. J Allergy Clin Immunol 1988;82:828-34.
  9. Fernadez J, Blanca M, Soriano V, Sanchez J, Juarez C. Epidemiological study of the prevalence of allergic reactions to Hymenoptera in rural population in the Mediterranean area. Clin Exp Allergy 1999;29:1069-74.
  10. Müller UR,. Entomology of the Hymentoptera. Clinical presentation and Pathogenesis. Diagnosis and Treatment Stuttgart, New York: Gustav Fischer, 1990, 3-65.
  11. Eich-Wanger C, Müller UR, Bee sting allergy in beekeepers. Clin Exp Allergy 1998;28:1292-98.
  12. Kettner A, Henry H, Hyghes G, Corradin G, Spertini F. IgE and T-cell responses to high-molecular weight allergens from bee venom. Clin Exp Allergy 1999;29:394-401.
  13. King T.P. Molecular approaches to the study of allergens. Monogr. Allergy 1990;28:84-100.
  14. Hoffman DR, Shipman WH, Babin B. Allergens in bee venom. II. Two new high molecular weight allergenic specificities. J Allergy Clin Immunol 1977;59:147-53.
  15. Sobotka A, Franklin R, Valentine M, Adkinson NF, Lichtenstein LM. Honey bee venom: Phospholipase A as the major allergen. J Clin Allergy Clin Immunol 1974;53:103.
  16. Hoffman DR, Shipman WH. Allergens in bee venom. I. Separation and identification of the major allergen. J Allergy Clin Immunol 1976;58:551-62.
  17. Arbesman CE, Reisman RE, Wypych JI. Allergenic potency of bee antigens measured by RAST inhibition. Clinical Allergy 1976;6:587-94.
  18. Sobotka AK, Franklin RM, Adkinson NF, Valentine MD, Baer H, Lichtenstein LM. Allergy to insect stings. II. Phospholipase A: The major allergen in honeybee venom. J Allergy Clin Immunol 1976;57:29-40.

As in all diagnostic testing, the diagnosis is made by the physican based on both test results and the patient history.