k224 rHev b 11 Latex

Allergens within Occupational Allergens

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  • Latin name: Hevea brasiliensis
  • Common names: Class 1 Chitinase
  • Source material: Recombinant non-glycosylated MBP fusion protein produced in an E. coli strain carrying a cloned cDNA encoding Hevea brasiliensis allergen Hev b 11
Recombinant allergen
Hevea brasiliensis allergen Hev b 11. 
 
Biological function
Chitinase plant defence
 
Mw
31.6 kD
 
Allergen description
Hev b 11 (1-2) is a class 1 chitinase with an N-terminal chitin-binding domain with homology to hevein (3). Heb v 11 shows greater than 65% identity with several other plant endochitinases (4). Chitinases are abundant proteins found in a wide variety of seed-producing plants. Most chitinases hydrolytically degrade chitin which is a major structural component of the cell wall of many fungi and the exoskeleton of many insects (3).
 
rHev b 11.0102 has been reported to have a 56% homology to hevein. rHev b 11.0102-specific IgE antibodies were found in 17 of 58 sera (29%) of IgE-mediated Latex-allergic subjects. Due to its IgE-reactivity, rHev b 11.0102 was reported to represent an allergen of intermediate prevalence in Natural rubber Latex (NRL), and it was stated that its cross-reactive potential with certain fruit makes it an important supplement in the diagnostic panel of recombinant NRL allergens (1).
 
Class I chitinases from Chestnut, Avocado and Banana have been identified as relevant allergens. The chitin binding (hevein) domain from these class I chitinases is thought to contain the important IgE binding epitopes. The H. brasiliensis chitinase, Hev b 11, was shown to have a 70% identity with the endochitinase from Avocado, and the identity was 58% between its hevein domain and Hev b 6.02 (hevein). rHev b 11 bound IgE antibodies in Latex- and fruit-allergic patients in 19% of 57 patients. The study concluded that Hev b 11, although having a chitin-binding domain, displays a different IgE binding capacity compared with hevein (2).
 
Similarly, a study of class I chitinases, evaluated for their potential role as cross-reactive allergens in Latex-food allergy, found polyclonal antibodies to chitinases in sera from patients with Latex-fruit allergy; the antibodies were in response to chitinases of Chestnut, Cherimoya, Passion fruit, Kiwi, Papaya, Mango, Tomato, and Wheat flour extracts. Prs a 1, the major allergen and class I chitinase from Avocado, was shown to strongly or fully inhibited the IgE binding of Latex chitinase. The study concluded that putative class I chitinases appear to be relevant cross-reactive components in foods associated with Latex-fruit syndrome, but do not play a specific role in allergy to Latex without a concomitant allergy to fruit (5).
 
Cross-reactivity has been described between Obeche wood dust and Latex. The Obeche allergen, Trip s 1, a class I chitinase, was homologous to Latex hevein (6).
 
Japanese cedar (Cryptomeria japonica) pollen allergy is one of the most prevalent allergic diseases in Japan. The cDNA high-frequency IgE-binding protein (CJP-4) cloned from C. japonica pollen was reported to have significant sequence homology to class IV chitinases and was able to bind IgE antibodies from all 31 patients tested by ELISA. Pre-incubation with Latex C-serum completely inhibited the reaction to purified CJP-4 of pooled sera IgE from patients with C. japonica pollinosis and/or Latex allergy (7).

References:

      1. Rihs HP, Dumont B, Rozynek P, Lundberg M, Cremer R, Bruning T, Raulf-Heimsoth M. Molecular cloning, purification, and IgE-binding of a recombinant class I chitinase from Hevea brasiliensis leaves (rHev b 11.0102). Allergy 2003;58(3):246-51.
      2. O'Riordain G, Radauer C, Hoffmann-Sommergruber K, Adhami F, et al. Cloning and molecular characterization of the Hevea brasiliensis allergen Hev b 11, a class I chitinase. Clin Exp Allergy 2002;32(3):455-62.
      3. Sussman GL, Beezhold DH, Kurup VP. Allergens and natural rubber proteins. J Allergy Clin Immunol 2002;110(2 Pt 2):S033-9.
      4. Yeang HY. Natural rubber latex allergens: new developments. Curr Opin Allergy Clin Immunol 2004;4(2):99-104.
      5. Diaz-Perales A, Collada C, Blanco C, Sanchez-Monge R, et al. Cross-reactions in the latex-fruit syndrome: A relevant role of chitinases but not of complex asparagine-linked glycans. J Allergy Clin Immunol 1999;104(3 Pt 1):681-7.
      6. Kespohl S, Sander I, Merget R, Petersen A, Meyer HE, Sickmann A, Bruening T, Raulf-Heimsoth M. Identification of an obeche (Triplochiton scleroxylon) wood allergen as a class I chitinase. Allergy 2005;60(6):808-14.
      7. Fujimura T, Shigeta S, Suwa T, Kawamoto S, Aki T, Masubuchi M, Hayashi T, Hide M, Ono K. Molecular cloning of a class IV chitinase allergen from Japanese cedar (Cryptomeria japonica) pollen and competitive inhibition of its immunoglobulin E-binding capacity by latex C-serum. Clin Exp Allergy 2005;35(2):234-43.

2006



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