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Hev b 8, the Hevea brasiliensis Latex Profilin, Is a Cross-Reactive Allergen of Latex, Plant Foods and Pollen.

Authors :
Ganglberger, Erika
Radauer, Christian
Wagner, Stefan
Ríordáin, Gabriel Ó
Beezhold, Donald H.
Brehler, Randolf
Niggemann, Bodo
Scheiner, Otto
Jensen-Jarolim, Erika
Breiteneder, Heimo
Source :
International Archives of Allergy & Immunology. 2001, Vol. 125 Issue 3, p216-227. 12p.
Publication Year :
2001

Abstract

Background: Plant profilins are important pan-allergens. They are responsible for a significant percentage of pollen-related allergies. Limited information is available about their involvement in the latex-fruit syndrome and the cross-reactivities between latex and pollen. We aimed to clone and express the Hevea brasiliensis latex profilin to investigate its allergological significance and serological cross-reactivities to profilins from plant foods and pollens. Methods: A DNA complementary to messenger RNA (cDNA) coding for the Hevea latex profilin, Hev b 8, was amplified by polymerase chain reaction from latex RNA. Recombinant (r)Hev b 8 was produced in Escherichia coli and used to screen sera from 50 latex- allergic health care workers (HCWs) with well-documented histories of food and pollen allergy and 34 latex-allergic spina bifida (SB) patients. The cross-reactivity of natural Hev b 8 and rHev b 8 with other plant profilins was determined by ELISA inhibition assays. A three-dimensional homology model of Hev b 8 was constructed based on known profilin structures. Results: The cDNA of Hev b 8 encoded a protein of 131 amino acids with a predicted molecular mass of 14 kD. Twelve of the 50 HCWs and 2 of the 34 SB patients were sensitized to Hev b 8. All Hev b 8-sensitized patients showed allergic symptoms to pollen or plant foods. Cross-reactivities between profilins of latex, pollen and plant food were illustrated by their ability to inhibit IgE binding to rHev b 8. Homology modeling of Hev b 8 yielded a structure highly similar to Bet v 2, the birch pollen profilin, with the most distinct differences located at the N-terminus. Conclusions: We conclude that primary sensitization to latex profilin in the majority of cases takes place via pollen or food profilins. Additionally, pollinosis and food-allergic patients with profilin-specific IgE can be at risk of developing latex allergy.Copyright © 2001 S. Karger AG, Basel [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
10182438
Volume :
125
Issue :
3
Database :
Academic Search Index
Journal :
International Archives of Allergy & Immunology
Publication Type :
Academic Journal
Accession number :
11335186
Full Text :
https://doi.org/10.1159/000053819