Allergy information for: Garden plum (Prunus domestica )

Name: Garden plum
Scientific Name: Prunus domestica
Occurrence: As fruit, juices, jams, jellies, preserves.
Allergy Information:
Like many other allergies to fresh fruits and vegetables, plum allergy can take two different forms. In the North of Europe, people with birch-pollen allergy can develop a plum allergy due to the similarity between a protein in birch that causes birch-pollen allergy, and a plum protein. This is called the birch-fruit syndrome with symptoms generally appearing within 5-15 min after consuming raw plum and comprising local reactions in the mouth and throat with itching and inflammation (called oral allergy syndrome, OAS). The molecule, known as an allergen, involved in this kind of allergy does not survive cooking. Therefore, people who react to this allergen can tolerate cooked plum. Individuals often develop adverse reactions to other fruits including apple, pear, apricot, cherry, melon, banana, nuts such as hazelnut, or vegetables such as celeriac (celery tuber) and carrot.
In Mediterranean countries, people with plum allergy do not have birch-pollen allergy. Instead they often have allergy to peach. Symptoms are more severe including generalised urticaria, abdominal pain, vomiting and life-threatening symptoms, sometimes in addition to the OAS. These individuals tend to have more frequent and severe reactions when fruits are eaten with the peel. They also tend to develop adverse reactions to other fruits including apple, peach, apricot, cherry and nuts (such as hazelnut and walnut). The allergen that causes this kind of allergy is tough and the allergenicity survives in processed foods such as juices. As a result, individuals with this kind of allergy cannot eat even cooked plum.
Other Information:
Taxonomic Information: NEWT http://www.ebi.ac.uk/newt/display?from=null&search=3758
Last modified: 18 October 2006

Reviews (0)

References (0)

Clinical History

Number of Studies:1-5
Number of Patients:>50
Symptoms:
Oropharyngeal symptoms characteristic of the oral allergy syndrome (OAS) (Pastorello et al. 1994) [156], (Pastorello et al. 2001) [152]

In addition, Rodriguez et al. (2000) [491] described gastrointestinal symptoms and generalised anaphylaxis

Skin Prick Test

Number of Studies:1-5
Food/Type of allergen:
Fresh fruit and commercial plum extracts (Pastorello et al. 1994) [156]

Commercial plum extract (Asero et al. 2000) [10]

Fresh fruit (Rodriguez et al. 2000) [491]
Protocol: (controls, definition of positive etc)
Pastorello et al. 1994 [156] used histamine dihydrochloride (10 mg/mL) as a positive control, and the glycerol-containing diluent of the prick solution as a negative control. A wheal graded at least 2+was regarded as positive.

SPT were carried out on the volar side of the forearm with a sterile, 1 mm-tip lancet pricking through the drop of the extract. Readings were taken after 15 min. Histamine (10 mg/mL) and saline solution were used as positive and negative controls repectively. Wheals with a diameter below 50% of the positve control were considered negative. (Asero et al. 2000) [10].

SPT were carried out by the prick-prick technique. Histamine (10 mg/mL) and saline solution were used as positive and negative controls repectively. A positive skin prick test result was defined as a mean (average of orthogonal to largest diameter) wheal of 3 mm or greater (after subtracting the diameter of the wheal induced by the diluent control). (Rodriguez et al. 2000) [491]
Number of Patients:
21 patients (Pastorello et al. 1994) [156]

498 patients (Asero et al. 2000) [10]

28 patients (Rodriguez et al. 2000) [491]
Summary of Results:
All patients of Pastorello et al. 1994 [156] showed a positive SPT.

49 patients (10%) had a positive SPT (Asero et al. 2000) [10]

Skin prick tests were positive in 19 patients (Rodriguez et al. 2000) [491]

IgE assay (by RAST, CAP etc)

Number of Studies:0
Food/Type of allergen:Commercial extracts (Rodriguez et al. 2000) [491], (Pastorello et al. 2001) [152]
IgE protocol:CAP (Rodriguez et al. 2000) [491], (Pastorello et al. 2001) [152]
Number of Patients:
28 patients (Rodriguez et al. 2000) [491]

23 patients (Pastorello et al. 2001) [152]
Summary of Results:
16 out of 28 patients had specific IgE to plum (Rodriguez et al. 2000) [491]

All patients had specific IgE to plum (Pastorello et al. 2001) [152]

Immunoblotting

Immunoblotting separation:
The extracts were separated in a discontinuous buffer system in an SDS-polyacrylamide gradient gel with a 6% stacking gel and a 7.5% to 20% separation gradient. Samples were boiled and reduced with beta-mercaptoethanol (Pastorello et al. 1994) [156]
Immunoblotting detection method:
The proteins were electroblotted to a nitrocellulose membrane, pore size 0.2 to 0.45 µm using a Trans-Blot Cell. The membrane was blocked with phosphate-buffered saline pH 7.4 with 0.5% (v/v) Tween 20 and incubated with the sera (diluted 1:4, v/v). The IgE-binding components were detected with iodine 125–labeled anti-human IgE antiserum diluted 1:4 (Pastorello et el. 1994) [156].
Immunoblotting results:
87% of sera (14 of 16) of Pastorello et al. 1994 [156], showed Ig E binding to a 13 kDa protein and 77% (14 of 18) to a 30 kDa protein . The other IgE -binding components were: 70 kDa (5 of 16, 31%), 20 kDa (6 of 16, 37%), 14 kDa (6 of 16, 37%), 40 kDa (6 of 16, 37%), 30 kDa (3 of 16, 18.7%) and 48 kDa (3 of 16, 18.7%). These bands were detectable in all but one patient with negative responses to birch pollen.

Oral provocation

Number of Studies:1-5
Food used and oral provocation vehicle:
Plum (Pastorello et al. 1994) [156], (Pastorello et al. 2001) [152]

A total of 17 g of dehydrated whole fruit was masked in a mix of orange (200 mL) and pineapple (200 mL) juices, sugar (16 g), wheat meal (13 g), and liquid coloring (Rodriguez et al. 2000) [491]
Blind:
Open (Pastorello et al. 1994) [156], (Pastorello et al. 2001) [152]

Open and DBPCFC (Rodriguez et al. 2000) [491]
Number of Patients:
21 patients (Pastorello et al. 1994) [156]

23 patients (Pastorello et al. 2001) [152]
28 patients with positive skin prick tests or CAP to Rosaceae fruits (Rodriguez et al. 2000) [491]
Dose response:
Patients chewed the fruit for 1 minute and then spat it out. If no symptoms appeared within 15 minutes, the challenge was repeated with increasing amounts from 250mg up to 64 g. Patients were asked not to spit out the last two doses but to swallow the fruit instead. (Pastorello et al. 1994) [156]. The same protocol was used by Pastorello et al. (2001) [152] but using doses from 4g up to 64 g.
Symptoms:
Oropharyngeal sympotoms (itching or tingling of the lips or oral mucosa) in 8 patients (Pastorello et al. 1994) [156]

All the patients showed oral allergy syndrome (OAS) (Pastorello et al. 2001) [152]
2 patients had oropharyngeal symptoms to plum, one had gastrointestinal symptoms and another one generalised anaphylaxis (Rodriguez et al. 2000) [491]

IgE cross-reactivity and Polysensitisation

Clinically relevant cross-reactivity between plum and peach has been observed by immunoblot inhibition (Pastorello et al. 1994) [156] (Pastorello et al. 2001) [152]

Other Clinical information

Reviews (0)

References (4)

Rodriguez J; Crespo JF; Lopez-Rubio A; de la Cruz-Bertolo J; Ferrando-Vivas P; Vives R; Daroca P
Clinical cross-reactivity among foods of the Rosaceae family.
J Allergy Clin Immunol 106:183-189. 2000
PUBMEDID: 10887323
Pastorello EA, Ortolani C, Farioli L, Pravettoni V, Ispano M, Borga A, Bengtsson A, Incorvaia C, Berti C, Zanussi C.
Allergenic cross-reactivity among peach, apricot, plum, and cherry in patients with oral allergy syndrome: an in vivo and in vitro study.
J Allergy Clin Immunol 94(4):699-707. 1994
PUBMEDID: 7930303
Asero R, Mistrello G, Roncarolo D, de Vries SC, Gautier MF, Ciurana CL, Verbeek E, Mohammadi T, Knul-Brettlova V, Akkerdaas JH, Bulder I, Aalberse RC, van Ree R.
Lipid transfer protein: a pan-allergen in plant-derived foods that is highly resistant to pepsin digestion.
Int Arch Allergy Immunol. 122:20-32.. 2000
PUBMEDID: 10859466
Pastorello EA, Farioli L, Pravettoni V, Giuffrida MG, Ortolani C, Fortunato D, Trambaioli C, Scibola E, Calamari AM, Robino AM, Conti A.
Characterization of the major allergen of plum as a lipid transfer protein.
J Chromatogr B Biomed Sci Appl 756(1-2):95-103. 2001
PUBMEDID: 11419731

Biochemical Information for Pru d 3

Allergen Name:Pru d 3
Alternatve Allergen Names:non specific lipid transfer protein (nsLTP)
Allergen Designation:Major
Protein Family:
Protease inhibitor/seed storage/LTP family, Pfam PF00234
non specific lipid transfer protein (nsLTP)
Sequence Known?:
Yes
Allergen accession No.s:
P82534:Swissprot: http://ca.expasy.org/cgi-bin/niceprot.pl?P82534
3D Structure Accession No.:Not determined
Calculated Masses:
9174 Da
Experimental Masses:9 kDa
Oligomeric Masses:None
Allergen epitopes:Not known
Allergen stability:
Process, chemical, enzymatic:
Not known but likely to be thermostable and resistant to proteases as other members of the nsLTP family (Asero et al. 2000) [10]
Nature of main cross-reacting proteins:There is extensive evidence of cross-reactivity amongst lipid transfer proteins from Rosaceae fruit (including apple, peach, apricot, cherry, plum, and pear) (Pastorello et al. 1994) [156].
Allergen properties & biological function:Plant nonspecific lipid-transfer proteins are thought to be involved in transport of fatty acids both intracellular and extracellularly and of cutin monomers to the cuticular layer of leaves and fruits. There is an expandable cavity between the four alpha-helices which can bind one or two lipids. nsLTPs have also been reported to act as plant defense proteins against bacterial and fungal infections and form the PR14 family of pathogenesis related proteins. (Lindorff-Larsen et al. 2001 [903]).
Allergen purification:250 g of plum peel is homogenised in 100 ml of 10 mM phosphate buffered saline pH 7 with 2% (w/v) polyvinylpolypyrrolidone, 2 mM EDTA and 10 mM diethyldithiocarbamate. After homogenizing and centrifuging, the resulting supernatant was dialysed and concentrated to 130 mg/ml. The solution was diluted 1:3 (v/v) with 30 mM sodium citrate pH 2.2 and loaded onto a Resource-S column for cation exchange. Elution used a gradient of 15 column volumes to 30 mM sodium citrate pH 2.2 with 1M NaCl. Concentrated fractions were loaded on a Superdex 75 gel filtration column (Pastorello et al. 2001) [152]
Other biochemical information:

References (4)

Asero R, Mistrello G, Roncarolo D, de Vries SC, Gautier MF, Ciurana CL, Verbeek E, Mohammadi T, Knul-Brettlova V, Akkerdaas JH, Bulder I, Aalberse RC, van Ree R.
Lipid transfer protein: a pan-allergen in plant-derived foods that is highly resistant to pepsin digestion.
Int Arch Allergy Immunol. 122:20-32.. 2000
PUBMEDID: 10859466
Pastorello EA, Farioli L, Pravettoni V, Giuffrida MG, Ortolani C, Fortunato D, Trambaioli C, Scibola E, Calamari AM, Robino AM, Conti A.
Characterization of the major allergen of plum as a lipid transfer protein.
J Chromatogr B Biomed Sci Appl 756(1-2):95-103. 2001
PUBMEDID: 11419731
Pastorello EA, Ortolani C, Farioli L, Pravettoni V, Ispano M, Borga A, Bengtsson A, Incorvaia C, Berti C, Zanussi C.
Allergenic cross-reactivity among peach, apricot, plum, and cherry in patients with oral allergy syndrome: an in vivo and in vitro study.
J Allergy Clin Immunol 94(4):699-707. 1994
PUBMEDID: 7930303
Lindorff-Larsen K, Lerche MH, Poulsen FM, Roepstorff P, Winther JR.
Barley lipid transfer protein, LTP1, contains a new type of lipid-like post-translational modification.
J Biol Chem. 276(36):33547-33553.. 2001
PUBMEDID: 11435437