Class I endochitinase containing a hevein domain is the causative allergen in latex-associated avocado allergy


Posch Toplab GmbH, Fraunhoferstraße 18a, D-82152 Martinsried, Germany.



In the medical literature immunoglobulin (Ig)E-mediated sensitization to avocado is rarely reported. On the other hand, more than 50% of subjects having IgE-mediated natural rubber latex allergy are sensitized to avocado fruit as demonstrated by skin-prick testing and/or specific IgE measurements and about 10–20% report hypersensitivity reactions after ingesting avocado.


The underlying pathomechanism of latex-associated avocado allergy is still unknown. The conserved hevein domain of the major latex allergen prohevein (Hev b 6.01) is a ubiquitous chitin-binding protein structure that can be found in several plant proteins and may be responsible for the observed cross-reactivity between latex and avocado fruit.


Chitin-binding avocado proteins (CBAPs) were isolated by affinity-chromatography and their IgE-binding characteristics were studied by immunoblotting using the sera from 15 avocado-sensitized latex patients. Inhibition experiments using isolated hevein and CBAPs as inhibitor solutions were performed to study the immunological cross-reactivity between both protein species and to assess the role of the CBAPs as mediators in latex-associated avocado allergy.


In 80% of avocado-sensitized subjects (n = 15), IgE antibodies directed against a 31-kDa allergen were detected by immunoblotting. This IgE-binding protein was identified by protein sequencing to be a class I endochitinase containing a hevein domain at the N-terminus. Purified native and digested (using simulated gastric fluid) endochitinase were able to completely block all avocado-specific IgE antibodies in six out of seven avocado patients.


Sensitization to endochitinase class I containing a hevein domain is the main underlying pathomechanism in latex-mediated avocado allergy.