CROSS-REACTIVITY OF FOOD ALLERGENS WITH LATEX - DIAGNOSTIC AND CLINICAL IMPLICATIONS

Considerable efforts have been undertaken to characterise the molecular features of Hevea brasiliensis latex allergens as a result of the high prevalence of latex allergy in well-defined risk groups such as health-care workers (HCW) and children with spina bifida (SB). Most of the latex allergens have been purified to homogeneity by conventional purification methods or by molecular cloning techniques. The clear advantage of recombinant proteins in contrast to native proteins is that it is possible to produce large-scale quantities at high reproducible quality. Several latex allergens have sequence homology to other allergens (like chitinases, enolase, profilin, patatin-like protein) while others are unique and do not share any similarity. Some of these allergens are responsible for the so called 'latex-fruit syndrome'. With the knowledge and use of the single allergens it is possible to improve the in vivo and in vitro diagnosis and establish a component-resolved diagnostic approach as prerequisite for specific immunotherapy strategies.

[1]  S. Scheurer,et al.  Relevance of the recombinant lipid transfer protein of Hevea brasiliensis: IgE-binding reactivity in fruit-allergic adults. , 2006, Annals of allergy, asthma & immunology : official publication of the American College of Allergy, Asthma, & Immunology.

[2]  A. Enk,et al.  In vitro hymenoptera venom allergy diagnosis: improved by screening for cross‐reactive carbohydrate determinants and reciprocal inhibition , 2006, Allergy.

[3]  T. Brüning,et al.  The new Hev b 7.02 iso‐allergen from Heve brasiliensis is an important allergen for health care workers and spina bifida patients , 2006, Allergy.

[4]  S. Wagner,et al.  Hevea brasiliensis Latex Allergens: Current Panel and Clinical Relevance , 2005, International Archives of Allergy and Immunology.

[5]  H. Yeang Natural rubber latex allergens: new developments , 2004, Current opinion in allergy and clinical immunology.

[6]  Monika Raulf-Heimsoth,et al.  Latex: a new target for standardization. , 2003, Arbeiten aus dem Paul-Ehrlich-Institut (Bundesamt fur Sera und Impfstoffe) zu Frankfurt a.M.

[7]  T. Brüning,et al.  Anaphylactic reaction to apple juice containing acerola: cross-reactivity to latex due to prohevein. , 2002, The Journal of allergy and clinical immunology.

[8]  H. Rihs,et al.  Recombinant spiked allergen extract , 2001, Allergy.

[9]  H. Rihs,et al.  Allergenicity of rHev b 10 (manganese‐superoxide dismutase) , 2001, Allergy.

[10]  H. Rihs,et al.  PCR‐based cloning, isolation, and IgE‐binding properties of recombinant latex profilin (rHev b 8) , 2000, Allergy.

[11]  Baur,et al.  Class I endochitinase containing a hevein domain is the causative allergen in latex‐associated avocado allergy , 1999, Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology.

[12]  T. Carrillo,et al.  Class I chitinases as potential panallergens involved in the latex-fruit syndrome. , 1999, The Journal of allergy and clinical immunology.

[13]  T. Carrillo,et al.  Latex allergy: clinical features and cross-reactivity with fruits. , 1994, Annals of allergy.