Hev b 8, the Hevea brasiliensis latex profilin, is a cross-reactive allergen of latex, plant foods and pollen

被引:80
作者
Ganglberger, E
Radauer, C
Wagner, S
O' Ríordáin, G
Beezhold, DH
Brehler, R
Niggemann, B
Scheiner, O
Jensen-Jarolim, E
Breiteneder, H
机构
[1] Univ Vienna, Dept Pathophysiol, A-1090 Vienna, Austria
[2] Guthrie Res Inst, Sayre, PA USA
[3] Univ Munster, Dept Dermatol & Venerol, D-4400 Munster, Germany
[4] Childrens Hosp, Virchow Clin, Berlin, Germany
关键词
recombinant Hev b 8; profilin; latex allergy; Hevea brasiliensis; cross-reactivity;
D O I
10.1159/000053819
中图分类号
R392 [医学免疫学];
学科分类号
100102 ;
摘要
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 (C) 2001 S. Karger AG, Basel.
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页码:216 / 227
页数:12
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