BACKGROUND: Anisakis simplex is a fish parasite that can cause allergy in humans. The multiple cross-reactivities of this nematode make diagnostic tests for allergy unreliable, because of frequent false-positive results. To date, only four allergens of A. simplex have been characterized, but their role in cross-reactivity is largely unknown. METHODS: We performed an amino acid sequence homology analysis, according to the Food and Agriculture Organization/World Health Organization (FAO/WHO) criteria, to identify allergens likely to be cross-reactive with Ani s 2 (paramyosin) and Ani s 3 (tropomyosin) of A. simplex. Next, within segments shared by Ani s 2 or Ani s 3 and homologous proteins, we searched for the occurrence of binding motifs of human leukocyte antigen (HLA) alleles (DRB1*1502, DQB1*0601, or DRB1*0404) known to be genetic risk factors for the development of allergy to A. simplex. RESULTS: We identified a number of proteins belonging to various organisms, which are significantly similar to (and therefore are likely to cross-react with) Ani s 2 and Ani s 3. The presence of binding motifs of HLA DRB1*0404 in Ani s 2, Ani s 3, and homolog proteins also supports our hypothesis. CONCLUSIONS: Our results provide a possible molecular explanation of some cross-reactivities reported for A. simplex, and suggest additional ones.
Cross-reactivity of Anisakis simplex: possible role of Ani s 2 and Ani s 3.
GUARNERI, Fabrizio Nicola Giuseppe;GUARNERI, Claudio;BENVENGA, Salvatore
2007-01-01
Abstract
BACKGROUND: Anisakis simplex is a fish parasite that can cause allergy in humans. The multiple cross-reactivities of this nematode make diagnostic tests for allergy unreliable, because of frequent false-positive results. To date, only four allergens of A. simplex have been characterized, but their role in cross-reactivity is largely unknown. METHODS: We performed an amino acid sequence homology analysis, according to the Food and Agriculture Organization/World Health Organization (FAO/WHO) criteria, to identify allergens likely to be cross-reactive with Ani s 2 (paramyosin) and Ani s 3 (tropomyosin) of A. simplex. Next, within segments shared by Ani s 2 or Ani s 3 and homologous proteins, we searched for the occurrence of binding motifs of human leukocyte antigen (HLA) alleles (DRB1*1502, DQB1*0601, or DRB1*0404) known to be genetic risk factors for the development of allergy to A. simplex. RESULTS: We identified a number of proteins belonging to various organisms, which are significantly similar to (and therefore are likely to cross-react with) Ani s 2 and Ani s 3. The presence of binding motifs of HLA DRB1*0404 in Ani s 2, Ani s 3, and homolog proteins also supports our hypothesis. CONCLUSIONS: Our results provide a possible molecular explanation of some cross-reactivities reported for A. simplex, and suggest additional ones.Pubblicazioni consigliate
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