AF043: Hevein-like and class I/II chitinase

List allergens from this family:

Routes of exposure:
Include only IUIS approved allergens.

Biochemical properties

A number of plant and fungal proteins that bind N-acetylglucosamine (e.g. solanaceous lectins of tomato and potato, plant class I endochitinases, the wound-induced proteins hevein, win1 and win2, and the Kluyveromyces lactis killer toxin α-subunit) contain a hevein domain, a small domain stabilised by 4 disulfide bonds in one or more copies [1]. The hevein-like domain is thought to be involved in recognition or binding of chitin subunits.

Allergens from this family

The major latex allergen prohevein (Hev b 6.01) is composed of an N-teminal hevein-like domain and a C-terminal barwin domain. Upon wound-induced coagulation of the latex, the protein is cleaved into its constituent domains. The N-terminal domain, named hevein, contains the major part of the IgE binding sites of prohevein [2]. N-terminal hevein-like domains of class 1 chitinases from fruits such as avocado, banana, and chestnut are cross-reactive with hevein and thought to be responsible for frequent allergic reactions of latex-allergic patients to these fruits termed the latex-fruit syndrome [3]. However, the clinical relevance of IgE cross-reactivity between hevein and class I chitinases has been questioned [4].

An allergen (Bra r 2) with a prohevein-like domain composition was identified in turnip rape [5]. Wheat germ agglutinin (Tri a 18) consists of four hevein-like domains and is an IgE-binding protein of low allergenic significance. Cry j 4, a class IV chitinase from Japanese cedar was shown to bind IgE from a high proportion of patients and cross-reacts with Hevea latex [6].



  1. Wright HT, Sandrasegaram G, Wright CS:
    Evolution of a family of N-acetylglucosamine binding proteins containing the disulfide-rich domain of wheat germ agglutinin.
    J Mol Evol 1991, 33, 283-94. [PubMed]
  2. Alenius H, Kalkkinen N, Reunala T, Turjanmaa K, Palosuo T:
    The main IgE-binding epitope of a major latex allergen, prohevein, is present in its N-terminal 43-amino acid fragment, hevein.
    J Immunol 1996, 156, 1618-25. [PubMed]
  3. Blanco C:
    Latex-fruit syndrome.
    Curr Allergy Asthma Rep 2003, 3, 47-53. [PubMed]
  4. Radauer C, Adhami F, Furtler I, Wagner S, Allwardt D, Scala E, Ebner C, Hafner C, Hemmer W, Mari A, Breiteneder H:
    Latex-allergic patients sensitized to the major allergen hevein and hevein-like domains of class I chitinases show no increased frequency of latex-associated plant food allergy.
    Mol Immunol 2011, 48, 600-9. [PubMed] [Full Text]
  5. Hanninen AR, Mikkola JH, Kalkkinen N, Turjanmaa K, Ylitalo L, Reunala T, Palosuo T:
    Increased allergen production in turnip (Brassica rapa) by treatments activating defense mechanisms.
    J Allergy Clin Immunol 1999, 104, 194-201. [PubMed]
  6. 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, 234-43. [PubMed] [Full Text]


Links to Pfam

Family-defining Pfam domains (at least one of these domains is present in each family member):

Pfam domain Pfam clan
PF00182 Chitinase class I CL0037 Lysozyme-like superfamily
PF00187 Chitin recognition protein -
PF00967 Barwin family CL0199 Double Psi beta barrel glucanase

Links to Wikipedia


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