Table of Contents

t240 Ole e 9 Scientific Information Summary Epidemiology Environmental Characteristics Clinical Relevance Molecular Aspects Diagnostic Relevance Compiled By

Component

t240 Ole e 9

t240 Ole e 9 Scientific Information

Type:

Component

Name; WHO/IUIS:

Ole e 9

Biological function:

Glucanase

Allergen code:

t240

Molecular Weight:

46 kDa

Source Material:

Olive tree pollen allergen component

Other Names :

1,3-beta-glucanase

Summary

Ole e 9 is a component found in olive pollen with a molecular weight of 46 kDa. Olive pollen allergy is a frequent allergy affecting people in the Mediterranean region. During the peak olive pollen season when olive pollen counts are high, Ole e 9 has been known to cause sensitization among 50 % of allergic patients from this region). Ole e 9 is a marker of severe allergic reactions in olive pollen allergic patients causing mainly asthmatic symptoms. Furthermore, it is found to be associated with moderate-to-severe atopic dermatitis. Ole e 9 is cross-reactive with latex, vegetables (including potato), fruits (including tomato and banana) and Ole e 10, due to sequence homology.

Epidemiology

Worldwide distribution

In Spain, the second most prevalent cause of allergy after grasses is olive (1, 2). Ole e 9, a component of olive pollen, has been reported to induce sensitization among 50% of allergy patients from some Mediterranean regions when olive pollen counts are high (> 5000 grains per m3) during pollen season (3, 4). Compared to the olive pollen allergen Ole e 1, sensitization to Ole e 9 was lower (10.7%) in geographic areas where olive pollen counts were also low, but higher (over 35%) in areas with high olive pollen exposure (5).

Environmental Characteristics

Source and tissue

Ole e 9 is an allergen found in olive pollen (6). The detection of Ole e 9 is often challenging from the available antigenic extracts, therefore recombinant (r)Ole e 9 has been expressed using Pichia pastoris (P. pastoris) (2, 7, 8)

Clinical Relevance

Disease severity

Ole e 9 is a marker of severe allergic illness in olive pollen allergic patients (5, 9). Moreover, Ole e 9 sensitized patients are almost twice as likely to have asthmatic symptoms compared to only Ole e 1 sensitized patients (5).

Ole e 9 IgE recognition has been associated with atopic dermatitis (AD) (3). A study involving 588 patients (with 173 mild, 257 moderate, and 158 severe patients) with AD showed a significant correlation between rOle e 9 levels and the manifestation of AD. Furthermore, specific IgE to rOle e 9 was found to be prevalent in 36.7% of patients with severe AD (10).

Cross-reactive molecules

Ole e 9 comprises two independent domains, including the N-terminal domain (NtD; 320-350 amino acids) and the C-terminal domain (CtD; 100 amino acid). The rNtD-specific polyclonal antiserum and sera derived from patients with olive pollen allergy confirmed the presence of IgE and IgG reactive epitopes common to 1,3 β-glucanase in Ole e 9 and also in tomato, banana, potato, and latex extracts. Furthermore, the study highlights that 1,3 β-glucanase from different allergens can be involved in pollen-fruit-latex cross-reactivity (7).

Molecular Aspects

Biochemistry

Ole e 9 is a 46 kDa, elongated 1,3-β-glucanase, found to be responsible for the degradation of β-1,3 glucans such as callose (4, 11). Ole e 9 is made up of a single, glycosylated polypeptide chain with two independent domains (10 kDa and 36 kDa) (10, 11). The NtD contains a catalytic domain, and the CtD has a carbohydrate-binding domain (12), the latter belonging to the pathogenesis-related protein family 2 (PR-2), which might be involved in latex-pollen-vegetable food allergy syndrome (10).

Isoforms, epitopes, antibodies

Ole e 9.0101 is an isoallergen of Ole e 9 (13).

Cross-reactivity due to structural similarity

The CtD of Ole e 9 has sequence homology (53% identity) with Ole e 10, resulting in cross-reactivity between them (14, 15).

Diagnostic Relevance

Cross-Reactivity

Cross-reactivity has been observed between Ole e 9 and the extracts from latex, tomato, potato, and banana (7).

Compiled By

Author: Turacoz Healthcare Pvt. Ltd

Reviewer: Dr. Michael Thorpe

Last reviewed:February 2022

References

Villalba M, Rodriguez R, Batanero E. The spectrum of olive pollen allergens. From structures to diagnosis and treatment. Methods. 2014;66(1):44-54.
Rodriguez R, Villalba M, Batanero E, Palomares O, Salamanca G. Emerging pollen allergens. Biomed Pharmacother. 2007;61(1):1-7.
Scala E, Asero R, Niederberger V. EACCI Molecular Allergology User's Guide2016. 13 p.
Poncet P, Senechal H, Charpin D. Update on pollen-food allergy syndrome. Expert Rev Clin Immunol. 2020;16(6):561-78.
Barber D, de la Torre F, Feo F, Florido F, Guardia P, Moreno C, et al. Understanding patient sensitization profiles in complex pollen areas: a molecular epidemiological study. Allergy. 2008;63(11):1550-8.
Huecas S, Villalba M, Rodriguez R. Ole e 9, a major olive pollen allergen is a 1,3-beta-glucanase. Isolation, characterization, amino acid sequence, and tissue specificity. J Biol Chem. 2001;276(30):27959-66.
Palomares O, Villalba M, Quiralte J, Polo F, Rodriguez R. 1,3-beta-glucanases as candidates in latex-pollen-vegetable food cross-reactivity. Clin Exp Allergy. 2005;35(3):345-51.
Palomares O, Villalba M, Rodriguez R. The C-terminal segment of the 1,3-beta-glucanase Ole e 9 from olive (Olea europaea) pollen is an independent domain with allergenic activity: expression in Pichia pastoris and characterization. Biochem J. 2003;369(Pt 3):593-601.
Barber D, Polo F, Lombardero M, Villalba M, Rodriguez R. The importance of minor allergens in allergen standardization. Arb Paul Ehrlich Inst Bundesamt Sera Impfstoffe Frankf A M. 2006(95):128-34; discussion 34, 55.
Scala E, Abeni D, Guerra EC, Pirrotta L, Locanto M, Meneguzzi G, et al. beta-1,3-glucanase rOle e 9 and MnSOD rAsp f 6 IgE reactivity are the signature of atopic dermatitis in the Mediterranean area. Clin Exp Allergy. 2020;50(4):487-98.
Torres M, Palomares O, Quiralte J, Pauli G, Rodriguez R, Villalba M. An Enzymatically Active beta-1,3-Glucanase from Ash Pollen with Allergenic Properties: A Particular Member in the Oleaceae Family. PLoS One. 2015;10(7):e0133066.
Zamora-Carreras H, Torres M, Bustamante N, Macedo AL, Rodriguez R, Villalba M, et al. The C-terminal domains of two homologous Oleaceae beta-1,3-glucanases recognise carbohydrates differently: Laminarin binding by NMR. Arch Biochem Biophys. 2015;580:93-101.
WHO/IUIS. Ole e 9 2019 [cited 2021 15.09.2021]. Available from: http://www.allergen.org/viewallergen.php?aid=463.
Quiralte J, Llanes E, Barral P, Arias de Saavedra JM, Saenz de San Pedro B, Villalba M, et al. Ole e 2 and Ole e 10: new clinical aspects and genetic restrictions in olive pollen allergy. Allergy. 2005;60(3):360-5.
Quiralte J, Palacios L, Rodriguez R, Cardaba B, Arias de Saavedra JM, Villalba M, et al. Modelling diseases: the allergens of Olea europaea pollen. J Investig Allergol Clin Immunol. 2007;17 Suppl 1:24-30