Prohevein from the rubber tree (<i>Hevea brasiliensis</i>) is a major latex allergen

Alenius, Harri; Kalkkinen, Nisse; Lukka, Matti; Reunala, Timo; Turjanmaa, Kristiina; Mäkinen-Kiljunen, Soili; Yip, Esah; Palosuo, Timo

doi:10.1111/j.1365-2222.1995.tb01114.x

Cited by 132 publications

(104 citation statements)

References 16 publications

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“…3), a conserved domain of 43 amino acid residues found in several plant and fungal proteins that has a common binding specificity for oligosaccharides of N-acetylglucosamine (26). This domain is found in endochitinases (EC 3.2.1.14) from class I A, in a number of nonleguminous plant lectins, and in prohevein, a major allergen and wound-induced protein from natural rubber latex (27,28). Based on the amino acid motifs found in the sequence, Prs a 1 belongs to endochitinases from family 19 of glycosyl hydrolases or, alternatively, to class I endochitinases ( Fig.…”

Section: Ige Binding Analysis Of Avocadomentioning

confidence: 99%

Identification and Cloning of Prs a 1, a 32-kDa Endochitinase and Major Allergen of Avocado, and Its Expression in the Yeast Pichia pastoris

Sowka

Hsieh²,

Krebitz

et al. 1998

Journal of Biological Chemistry

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Avocado, the fruit of the tropical tree Persea americana, is a source of allergens that can elicit diverse IgE-mediated reactions including anaphylaxis in sensitized individuals. We characterized a 32-kDa major avocado allergen, Prs a 1, which is recognized by 15 out of 20 avocado-and/or latex-allergic patients. Natural Prs a 1 was purified, and its N-terminal and two tryptic peptide sequences were determined. We isolated the Prs a 1 encoding cDNA by PCR using degenerate primers and 5-rapid amplification of cDNA ends. The Prs a 1 cDNA coded for an endochitinase of 326 amino acids with a leader peptide of 25 amino acids. We expressed Prs a 1 in the yeast Pichia pastoris at 50 mg/liter of culture medium. The recombinant Prs a 1 showed endochitinase activity, inhibited growth and branching of Fusarium oxysporum hyphae, and possessed IgE binding capacity. IgE cross-reactivity with latex proteins including a 20-kDa allergen, most likely prohevein, was demonstrated, providing an explanation for the commonly observed cross-sensitization between avocado and latex proteins. Sequence comparison showed that Prs a 1 and prohevein had 70% similarity in their chitin-binding domains. Characterization of chitinases as allergens has implications for engineering transgenic crops with increased levels of chitinases.

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Section: Ige Binding Analysis Of Avocadomentioning

confidence: 99%

Identification and Cloning of Prs a 1, a 32-kDa Endochitinase and Major Allergen of Avocado, and Its Expression in the Yeast Pichia pastoris

Sowka

Hsieh²,

Krebitz

et al. 1998

Journal of Biological Chemistry

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“…Immunoglobulin G4 (IgG4) antibodies against NRL proteins have also been detected in the serum of NRL-sensitive subjects [36], but their pathophysiological relevance remains to be determined. Among the proteins identified in NRL, rubber elongation factor (14 kDa) and prohevein (20 kDa) have so far been documented as relevant allergens involved in IgE-mediated allergy to NRL [37,38]. Several reports indicate that NRL allergens may crossreact with latex from the weeping fig (Ficus benjamina) [39], and various fruits (banana, avocado, passion fruit, kiwi and chestnut) [40][41][42][43][44].…”

Section: Nrl Allergensmentioning

confidence: 99%

Occupational asthma caused by natural rubber latex

Vandenplas¹

1995

Eur Respir J

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O Oc cc cu up pa at ti io on na al l a as st th hm ma a c ca au us se ed d b by y n na at tu ur ra al l r ru ub bb be er r l la at te ex x Recent studies indicate that asthma is a frequent manifestation of NRL allergy among workers manufacturing NRL materials and among health-care providers using NRL gloves. NRL-induced asthma should receive increasing attention as it can lead to permanent respiratory sequelae and occupational disability. The need for early and accurate diagnosis is outlined and the different diagnostic approaches are reviewed. Specific issues pertaining to the management of affected subjects and to the prevention of exposure to airborne NRL are discussed.Areas of future research should include: 1) further characterization of relevant NRL allergens; 2) development and validation of methods for quantitative assessment of allergen content in NRL devices and workplace environments; 3) standardization of allergen extracts used for diagnostic purposes; 4) prospective evaluation of the natural history and risk factors of NRL-induced asthma; and 5) analysis of effectiveness and cost of preventive strategies.

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“…4; compare WT hevein and H⌬6). Three of the mutated residues are charged, Arg 5 , Lys 10 , and Glu 29 , and their substitution with alanine markedly changes the surface charge distribution (Fig. 4; compare WT hevein and H⌬6).…”

Section: Structural Studies and Molecular Modeling Of Combinatory Hevmentioning

confidence: 99%

“…Hevein is a small and stable protein that is recognized by ϳ70% of NRL allergic patients (10,11). Its 3-D structure has been solved (12,13) and several hevein homologues have been identified (14 -16).…”

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confidence: 99%

Construction of Hevein (Hev b 6.02) with Reduced Allergenicity for Immunotherapy of Latex Allergy by Comutation of Six Amino Acid Residues on the Conformational IgE Epitopes

Karisola

Mikkola

Kalkkinen

et al. 2004

The Journal of Immunology

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Recently we have established that IgE Abs bind to conformational epitopes in the N- and C-terminal regions of the major natural rubber latex allergen, hevein (Hev b 6.02). To identify the critical amino acid residues that interact with IgE, the hevein sequence was scanned by using site-specific mutations. Twenty-nine hevein mutants were designed and produced by a baculovirus expression system in insect cells and tested by IgE inhibition-ELISA using sera from 26 latex allergic patients. Six potential IgE-interacting residues of hevein (Arg5, Lys10, Glu29, Tyr30, His35, and Gln38) were identified and characterized further in detail. Based on these six residues, two triple mutants (HΔ3A, HΔ3B) and hevein mutant where all six residues were mutated (HΔ6), were designed, modeled, and produced. Structural and functional properties of these combinatory mutants were compared experimentally and in silico with those of recombinant hevein. The IgE-binding affinity of the mutants decreased by three to five orders of magnitude as compared with that of recombinant hevein. Skin prick test reactivity of the triple mutant HΔ3A was drastically reduced and that of the six-residue mutant HΔ6 was completely abolished in all patients examined in this study. The approach presented in this paper offers tools for identification and modification of amino acid residues on conformational epitopes of allergens that interact with IgE. Hevein with a highly reduced ability to bind IgE should provide a valuable candidate molecule for immunotherapy of latex allergy and is anticipated to have a low risk of systemic side effects.

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Prohevein from the rubber tree (Hevea brasiliensis) is a major latex allergen

Abstract: The observed high frequency of IgE antibodies to prohevein suggests that this protein is a major natural rubber latex allergen.

Cited by 132 publications

References 16 publications

Identification and Cloning of Prs a 1, a 32-kDa Endochitinase and Major Allergen of Avocado, and Its Expression in the Yeast Pichia pastoris

Identification and Cloning of Prs a 1, a 32-kDa Endochitinase and Major Allergen of Avocado, and Its Expression in the Yeast Pichia pastoris

Occupational asthma caused by natural rubber latex

Construction of Hevein (Hev b 6.02) with Reduced Allergenicity for Immunotherapy of Latex Allergy by Comutation of Six Amino Acid Residues on the Conformational IgE Epitopes

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