The pine processionary caterpillar is the larval form of the Thaumetopoea pityocampa moth. Mediterranean forests regularly suffer plagues of this insect, which has been moving north as a result of global warming. When the small urticating hairs that develop during the last 3 larval stages are shed and can become airborne. If they come in contact with skin, they can cause a variety of reactions, notably contact urticaria and papular rashes. Irritation can also occur if the hairs lodge in the mucosa of the conjunctiva or in the respiratory tract. Several cases of anaphylactic reactions have been reported in recent years. Mechanical (irritative) mechanisms may be involved in the pathogenesis of lesions, or immunoglobulin E-mediated allergic hypersensitivity reactions may be implicated when the process is rapid, recurrent, and progressively more severe.
DOI : 10.1016/j.adengl.2011.11.005 Anahtar Kelimeler :
Pine processionary caterpillar, Thaumetopoea pityocampa, Dermatitis, Urticaria, Oruga procesionaria del pino, Thaumetopoea pityocampa, Dermatitis, Urticaria
Cilt: 102 Sayı: 9 Sayfa: 658-667 ISSN: 1578-2190
In this study, we analyzed the presence of antibodies against the basement membrane antigen laminin (LMN) in patients with systemic lupus erythematosus (SLE), filariasis, and normal controls. By ELISA, 13.8% of SLE (12/87), 66.7% of parasitized patients (20/30), and two of the normal controls had these antibodies. IgG1 anti-LMN response was elevated in all groups, whereas IgG2 and IgG3 were also elevated in parasitized patients. The analysis of the IgG anti-laminin binding capacity in SLE and parasitized patients showed similar average antibody affinity. These antibodies did not react with fibronectin by a competition ELISA. By Western blot, the anti-laminin antibodies could be demonstrated in parasitized patient sera but not in SLE sera. Moreover, the ability of these antibodies to bind to heat-treated LMN (100°C for 4 min) was different. The study of the binding capacity with native or denatured LMN by Western blot and dot-blot assays showed that the anti-LMN antibodies from parasitized patients were able to react with both native and denatured forms of LMN, whereas in SLE patients these antibodies were demonstrated only with native LMN. On the other hand, the reactivity detected in the normal control sera seems to be different from the anti-LMN antibodies from SLE and parasitized patients, and probably reflects the existence of natural antibodies in these sera. The presence of anti-LMN antibodies correlates significantly with the ability of inhibition of U937 cell adhesion to LMN-coated surfaces (P < 0.0025). The difference of anti-laminin reactivity suggests that antibodies produced following immunization with autoantigens or similar molecules present in parasites have different specificities from those spontaneously produced by individuals with autoimmune diseases.
The antigenic sites on the major allergen from yellow mustard (Sinapis alba L.) seeds were studied using murine (BALB/c) monoclonal antibodies (mAb) and human IgE antibodies. Ten IgGl (K) mAb from two fusions were analyzed. Competition and complementation studies performed with peroxidase labeled mAb reveal the existence of two main antigenic sites in Sin a I. All the described mAb failed to recognize the unordered carboxyamidomethylated polypeptide chains, with the single exception of 2B3, which binds the alkylated large chain. However, this mAb cannot react with the tetranitromethanemodified protein which retains the native conformation. This fact suggests that the only tyrosine of 5m a I, located in the large chain, may be part of a sequential epitope of the allergen. This chemical modification also alters the binding of the mAb 4A11 and 3F3 to the allergen, besides 2B3. The three mAb belong to the same complementation group. Specific IgE binding cannot be inhibited either by the large or small carboxyamidomethylated polypeptide chains, while the nitrated allergen shows a weaker inhibitory activity than the native Sin a I. 4A11, which is a tyrosine-dependent mAb, causes the greatest binding inhibition of the tested mAb on human IgE from atopic individuals, as determined from a reverse enzyme immunoassay, suggesting an important role played by tyrosine in the immunochemical recognition of Sin a I.
Anisakis simplex is a fish parasite responsible for human infection and is able to induce IgE-mediated reactions with several clinical manifestations. Laboratory diagnosis of Anisakis allergy is based on the detection of specific IgE using parasite whole antigen. Unfortunately, these diagnostic tools detect cross-reactivities with other nematodes and micro-organisms leading to low specificity of the diagnostic tests. The aim of this retrospective study was to assess the diagnostic value of specific IgE to Anisakis for diagnosis of A. simplex-sensitization in native Spanish residents (IMM, n = 766) and subjects coming from tropical and sub-tropical geographic areas (TRO, n = 233). Since Ascaris is the human parasite most closely related to Anisakis, specific IgE to Ascaris was also determined to assess Anisakis cross-reaction with other nematodes and the diagnostic value of Anisakis/Ascaris IgE ratio for Anisakis allergy was examined. IMM and TRO groups showed similar specific IgE to Anisakis levels, while TRO had higher levels of specific IgE to Ascaris than IMM group (p = 0.001). ROC curve analysis determined that an Anisakis specific IgE threshold of 0.71 kU/L yielded 93% and 82% specificities in IMM and TRO groups, respectively. A cut-off value ≥4.4 for Anisakis/Ascaris IgE ratio increased specificity to 95% for samples having IgE to Ascaris ≥0.35. In conclusion, the ratio of specific IgE to Anisakis and Ascaris improved remarkably the specificity and this parameter easily obtained from the commercially available system could be useful in the diagnosis of hypersensitivity to A. simplex.