Latin name: Prunus persica
Source material: Fruit pulp
A food, which may result in allergy symptoms in sensitised individuals.
Peach, Prunus persica, is the fruit of a deciduous tree growing as high as 10 m and belonging to the sub-family Prunoideae of the family Rosaceae. It is classified with the almond in the subgenus Amygdalus, distinguished from the other subgenera by the corrugated seed shell. The peach is a tree native to China. It was introduced to Persia and the Mediterranean region through the Silk Road in early historical times, probably by about 2000 BC. Important historical peach-producing areas are China, Japan, Iran, and the countries in the Mediterranean region; and more recently, the US, Canada, and Australia.
The leaves are lanceolate, 7–15 cm long and 2–3 cm broad. The flowers are produced in early spring before the leaves; they are solitary or paired, 2.5–3 cm in diameter, pink, with 5 petals. Peaches, along with cherries, plums and apricots, are stone fruits (drupes). The fruit of all of these is roundish, with a single large seed encased in hard wood (called the ‘stone’ or ‘pit’). Peach skin is velvety, downy, and can be red, pink, yellow, white or any combination of these. It is often flushed with red, and bruises easily. On one side of the fruit is a distinctive vertical indentation. The pulp is yellow or whitish, highly flavoured, and sweet. The seed or ‘pip’ is red, oval-shaped and 1.5–2 cm thick.
Peach comes third in world production of deciduous tree fruits. Peaches are divided into ‘freestone’ and ‘clingstone’ cultivars, depending on whether the flesh sticks to the stone or not. These two types merge in some varieties, so that even the same trees may be freestone in one season and clingstone in another. Both kinds can have either white or yellow flesh. They are cultivated throughout warm-temperate and subtropical regions of the world. Nearly 300 varieties of peach are grown in America alone, each having its particular physical characteristics and ripening season.
The nectarine is a cultivar of peach that looks very similar, except that it has a smooth, shiny skin without fuzz (hair). Nectarines can be white, yellow, clingstone, or freestone. Ordinary peach trees occasionally produce a few nectarines, and vice versa.
Harvesting is done manually in summer, and storage is in cold rooms.
Peach is usually consumed fresh but may be canned, dried or pickled. Its classic uses are in pastries, but it also often features in chutneys and jams.
Several peach allergens of major importance have been detected, including a lipid transfer protein, a profilin, and many larger proteins. (1, 2)
The following allergens have been characterised:
Pru p 1, a 9 kDa protein, a Bet v 1 homologue, a Group 1 Fagales-related protein. (3, 4, 5, 6, 7, 8, 9, 10)
Pru p 2, a thaumatin-like protein (TLP). (3, 11, 12, 13, 14)
Pru p 3, a 9 kDa lipid transfer protein. (1, 2, 3, 4, 5, 6, 8, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45)
Pru p 4, a profilin. (2, 3, 4, 5, 7, 8, 15, 17, 46, 47)
Pru p 7, peamaclein, an anti-microbial peptide. (3, 48)
Pru p glucanase, a 1,3-beta-glucanase. (49, 50)
The allergen that was known as Pru p 1 has been renamed Pru p 3, and Pru p 1 is now the name for a Group 1 Fagales-related Protein, a Bet v 1 homologue. Pru p 1 and Pru p 3 are major allergens in peach fruit. Pru p 1 has low concentations and is highly labile, whereas Pru p 3 is highly abundant in peach peel and is heat- and gastric-acid stable. (4) Mean Pru p 3 levels were approximately 132, 0.6, and 17 microg/g of fresh weight of peels, pulps, and whole peach fruits, respectively, whereas mean Pru p 1 levels were 0.6, 0.3, and 0.1 microg/g of fresh weight. Most US peach cultivars showed higher levels of both allergens than Spanish cultivars. (5) LTP levels are also greatly dependent on maturity and storage conditions. (51)
Allergy to lipid transfer protein (LTP) is quite common in the Mediterranean countries, but virtually absent in Northern Europe. (52) Lipid transfer protein is associated with systemic reactions more severe than the milder symptoms such as oral allergy syndrome. Peach LTP (Pru p 3) is a minor allergen in Northern European countries but a major allergen in the South, affecting over 60% of patients allergic to peach in the Spanish population, and over 72% in the Italian population. (27) Of peach-allergic patients who have experienced systemic reactions to peach, up to 100% may be sensitised to LTP. (22)
Lipid transfer proteins (LTPs) concentrate in the skin of Rosaceae fruits as cell surface-exposed allergens. (1, 24) LTP is found in peach peel in concentrations approximately 7 times greater than in the pulp. LTP contents were as follows: yellow peach peel, 15.48; yellow peach pulp, 2.25; red peach peel, 14.67; and red peach pulp, 1.84. (21) The substance may be absent from chemically peeled fruit, and levels of LTP vary among cultivars and at different stages of the ripening process, showing a progressive increment during ripening. (53) A hypothesis that peach may lose its allergenicity (and therefore its primary role as a sensitiser to LTP) as a consequence of processing preceding marketing in Northern Europe was evaluated in a study. Peach surface fuzz reactivity in peach-allergic individuals was shown to be stronger than reactivity to peel. Pre-absorption of one serum with peach LTP caused an 87% reduction of IgE reactivity to peach fuzz extract. (52)
Pru p 4 is a member of the profilin plant family, allergens that bind IgE antibodies of almost 20% of plant-allergic patients. Human IgE reactivity to profilin appears to depend strongly on the highly conserved conformational structure, rather than on a high degree of amino acid sequence identity or even on the linear epitopes that have been identitied, as demonstrated in a study evaluating melon profilin. (54) Peach contains 2 profilin isoforms, Pru p 4.01 and Pru p 4.02, which show 80% amino acid sequence identity and are very similar (>70% identity) to allergenic profilins from plant foods and pollens. In a study of sera of 29 patients with peach allergy (confirmed by DBPCFC in evaluating recombinant peach profilin isoform reactivity), Pru p 4.01 was recognised by all sera (15 of 15) with specific IgE to Bet v 2, whereas no sera (0 of 14) without IgE to birch allergen reacted with rPru p 4.01. (47) In the Spanish population, where peach LTP is a major allergen, sensitisation to profilin is observed with an associated pollen allergy but does not appear to be related to clinical reactivity to peach. (27) This may differ in other countries, in particular in Southern Europe, where peach LTP is the dominant peach allergen.
A high level of cross-reactivity occurs among members of the Rosaceae family. (55) Allergy to fruits and vegetables is often associated with pollen allergy, but the relationship between fruit and pollen allergens is not simple. Cross-reactivity patterns observed differ between geographical areas and climates, depending on the differences in exposure to inhaled and ingested allergens. For example, the association between birch tree pollen allergy and peach allergy in Northern Europe (80) may be explained by the detection of a Bet v 1-related protein in peach, (2) whereas in Southern Europe and other countries, cross-reactivity associated with peach is more likely to be associated with other fruits and vegetables containing lipid transfer proteins. (52)
Pru p 3, a lipid transfer protein allergen, possibly along with other larger peach proteins, is involved in allergenic relations with other fruits from the family Rosaceae, particularly apricot, cherry, and plum. (1, 2, 56) A high level of cross-reactivity occurs between fruits and vegetables containing lipid transfer proteins, which include sweet chestnut, (57) cabbage (with 50% of identity to peach LTP), (58) walnut, (59) lettuce (60) and hazelnut. (61) Grapes and wine may contain lipid transfer protein homologous to and cross-reactive with peach LTP. (62) A report was made on a 19-year-old boy with a history of oral allergy syndrome who, after eating peach, presented with several episodes of generalised urticaria and angioedema approximately 15-20 minutes after drinking beer. The responsible allergen was found to be a lipid transfer protein from the barley that is present in beer. (63) Lipid transfer cross-reactivity is often accompanied by clinical food allergy, frequently including systemic reactions. (18)
In a study examining the relationship between peach LTP specific IgE levels and cross-reactivity to several non-Rosaceae plant-derived foods, patients with negative skin-specific IgE for non-Rosaceae foods showed significantly lower levels of IgE to peach LTP than did patients showing skin reactivity to 1 or more non-Rosaceae foods. Increasing levels of IgE to peach LTP were associated with skin reactivity to nuts (29/40 [72%]), peanut (27/40 [67%]), maize (16/39 [41%]), rice (14/39 [36%]), onion (13/37 [35%]), orange (9/32 [28%]), celery (11/40 [27%]), and tomato (8/39 [20%]). The study suggested that all allergenic determinants in LTP from vegetable foods other than peach cross-react with peach LTP, whereas only some peach LTP epitopes cross-react with allergenic determinants in botanically unrelated, plant-derived foods. The high levels of IgE to peach LTP seemed to reflect the presence of IgE that targeted common allergenic determinants of LTP, causing cross-reactivity to botanically unrelated plant foods. The authors concluded that in LTP-allergic patients, increasing levels of IgE to peach LTP are paralleled by an increasing number of foods other than Rosaceae triggering positive skin-specific IgE and causing clinical symptoms. (64)
Allergenic LTPs from peach fruit and mugwort (Artemisia vulgaris) pollen are responsible for clinical symptoms in Mediterranean patients, as a result of cross-reactivity. (57, 65 )A study was done to assess the pattern of sensitisation to an array of mugwort allergens in a Mediterranean population, and the cross-reactivity of Art v 3 (mugwort) with Pru p 3 and Par j 1 – all of these being relevant lipid LTP allergens in the area. The 3 Artemisia allergens elicited a positive skin-specific IgE response in 70-80% of the patients. Seven patients were clearly sensitised to Par j 1, and 11 to Pru p 3. There was no correlation between Par j 1 and Pru p 3 sensitisation, but a highly significant correlation was found between peach and Art v 3 with regard to skin-specific IgE. No IgE cross-reactivity was observed between Art v 3 and Par j 1 or between Pru p 3 and Par j 1. In contrast, Art v 3 significantly inhibited the binding to Pru p 3 of IgE from 3 patients' sera out of 6 studied, but Pru p 3 was not able to inhibit IgE binding to Art v 3. The study concludes that Art v 3 is a major mugwort allergen, and that in some patients with IgE to both Art v 3 and Pru p 3, Art v 3 behaves as the primary sensitising agent. (66)
Therefore, hypersensitivity to mugwort in patients with peach allergy is due to a common lipid transfer protein allergen, but is often without clinical expression. (67) This is illustrated by a study of 47 patients allergic to peach and 20 patients sensitised to mugwort pollen but with no clinical food allergies: the rate of positive skin-specific IgE for peach, apple, chestnut and mugwort LTPs were, respectively, 91, 77, 23, and 36% in the peach group, and 30, 5, 15 and 40% in the mugwort group. In peach-allergic patients, the most frequent pattern of cross-reactivity to LTPs appears to be the combination peach-apple (45%), followed by peach-apple-mugwort-sweet chestnut (21%). Significant correlation was found between peach and apple LTPs, and between mugwort and sweet Chestnut LTPs. (68) Importantly, the IgE-binding cross-reactivity due to fruit lipid transfer protein has varying degrees of clinical relevance, and this cross-reactivity is not necessarily accompanied by cross-allergenicity to the corresponding fruits. (29)
Cross-reactivity of lipid transfer proteins may therefore be complex. Mugwort Art v 3 and plane tree Pla a 3 are implicated in plant food-pollen co-censitisation, displaying partial cross-reactivity with peach Pru p 3 and other food allergens. Art v 3 shares 40% of its sequence with Pru p 3 and has an approximately 70% prevalence of specific IgE in Artemisia-allergic patients. However, sensitisation to Pla a 3 is low in plane tree pollen-allergic subjects without food allergy (27.3%), but high (> 60%) among those with associated peach allergy. (31) A second type of allergenic nonspecific LTP from pollens corresponds to ragweed Amb a 6 and olive Ole e 7, which are minor allergens. These present less than 35% sequence identity with Pru p 3, and have not been involved in pollen-plant food cross-reactivity. Par j 1 and Par j 2, the major allergens of Parietaria, represent a further type of nonspecific LTP member, with low levels of sequence identity (26–29%) with peach pulp 3, and no reported cross-reaction with any food or even pollen allergens (such as Art v 3) of the family. (69)
It has been suggested that the primary sensitiser to LTP is the peach, based on the following observations:
- Virtually no LTP-allergic patient not sensitised to peach has been reported so far; the few who showed no skin-specific IgE for peach had been tested with fresh fruit only, a method that in this particular type of food allergy is less sensitive than skin-specific IgE determination with commercial food extract;
- Peach-allergic, LTP-hypersensitive patients frequently tolerate other Rosaceae as well as non-Rosaceae plant foods, and are negative on skin- and serum-specific IgE evaluation with these foods;
- Cross-reactivity to non-Rosaceae plant foods is strongly dependent on the level of IgE to peach LTP. (52)
IgE antibodies to profilin seem to be responsible for at least part of the observed relationship between peach food allergy and allergy to grass and olive tree pollen in the Mediterranean area, where Betulaceae pollens in the air are rare or absent. (46, 83, 70, 71) Profilins are highly cross-reactive allergens, which bind IgE antibodies of almost 20% of plant-allergic patients. Melon profilin has been shown to have substantial cross-reactivity with profilins from peach, tomato, grape and Bermuda grass (Cynodon dactylon) pollen. (54)
A 1,3-beta-glucanase, isolated from olive tree pollen (Ole e 10) and shown to be a major allergen in Olive tree pollen-allergic patients, has been shown to be a panallergen with cross-reactivity to a number of pollens, and to fruits and vegetables such as tomato, kiwi, potato, and peach. This allergen was suggested as a strong candidate for involvement in pollen-latex-fruit syndrome. (49) Indeed, cross-reactivity with latex has been suggested. (72, 73)
A number of other reports have been published documenting cross-reactive relationships between peach on the one hand, and pollens and foods on the other, but the specific allergens were not characterised.
Cross-reactivity has been described between cypress pollen allergy and peach food allergy: 7 patients with cypress pollen allergy, with symptoms during winter, developed oral allergy, urticaria or oedema immediately following ingestion of peach. Cypress pollens and peach were shown to have common epitopes on allergens of 45 kDa molecular weight. (74)
A study of patients in Sapporo, Japan, found that among the 61% of a group of 54 patients with birch allergy, a high number were also allergic to fruits: apple (97%), peach (67%), cherry (58%), pear (40%), plum (40%) and melon (33%). (75) Similarly, in a Swiss study of the serum of 274 patients allergic to 1 or more of 3 pollens (birch, grass, mugwort), 111 patients (47%) were positive (> or = 0.71 kU/l) for a food allergen. Of these, 92 were sensitised to apple, 68 to potato, 64 to carrot, 63 to celery, 61 to peach, and 44 to melon. (76)
Cross-reactivity between raspberry and peach has been reported. (77)
a. IgE-mediated reactions
Peach is a well-documented and common cause of allergy in children and adults, resulting in oral allergy and systemic reactions such as urticaria, asthma and anaphylactic shock following the ingestion of the fresh or processed fruit. This is particularly the case in the Mediterranean area, where peach is regarded as a major allergen. (27, 47, 55, 68, 76, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87) Peach has also been described as the primary cause of food anaphylaxis in a number of countries, (7) including Israel. (84) In Japan, peach has been reported to be a frequent cause of oral allergy syndrome (OAS). (88, 89)
Peach allergy has 2 basic patterns: that of Central and Northern Europe, with OAS related to a primary sensitisation to birch pollen Bet v 1 and profilins; and that of Southern Europe, with mostly systemic symptoms, in many cases due to sensitisation to lipid transfer proteins. (32)
Patients in the Mediterranean area are invariably not allergic to birch tree pollen, and the main reactions are directed not to Bet v 1 homologues or profilin but to LTPs, as described above. (52) Allergic symptoms involving LTPs are more likely to be systemic and severe, and occur in addition to oral allergy syndrome. However, sensitisation to the lipid transfer protein Pru p 3 is rare among the Central and Northern European population. (22) There, allergy to peach and other Rosaceae fruits in patients with a related pollen allergy is a milder clinical entity, and profilin- and Bet v 1-related structures are involved. (90)
This is further illustrated by a study of 30 Spanish peach-allergic patients with positive skin and food challenge tests. Pru p 3 was the major allergen in the patient group from northern Spain, with sensitisation to this allergen occurring in all of the patients who had systemic symptoms or contact urticaria. Of the patients with OAS, all were sensitised to profilin, and 60% to allergens of the Bet v 1 family, with only 60% being sensitised to Pru p 3. Thus, in the northern Spanish patients, there was a mixed Central-South European pattern, with LTP-profilin-Bet v 1 sensitisation, and with the symptoms depending on individual profiles. (32)
In a study of lettuce allergy involving 29 lettuce-allergic patients, with or without concomitant peach allergy, and 19 peach-allergic patients without lettuce allergy, out of the total peach-allergic patients (23 + 19), 2 had experienced anaphylaxis, 13 OAS, 13 urticaria, 9 angioedema, 1 contact urticaria, and 1 rhinoconjunctivitis. (91)
Even young infants may experience allergic symptoms, as described in an infant of 4 months who developed urticaria and anaphylaxis following the ingestion of peach. (82) Peach is also among a number of foods causing multifood allergy, as described in a 4-year-old child. (92) Anaphylaxis may occur in a biphasic manner. (93)
Contact urticaria from peach skin has been described. (94) In particular, LTP-allergic patients frequently report local urticaria or pruritus upon contact with fresh peaches; in a Spanish study (notably, in a geographic area where birch trees are virtually absent and the prevalence of allergy to LTP is very high), 61% of 70 peach-allergic subjects had contact urticaria from peaches, and this was the most frequent symptom of peach allergy after oral allergy syndrome. Oral allergy syndrome affected 86% of the study group, followed by contact urticaria (61%) and systemic symptoms (26%). Approximately 67% of the patients were allergic to peach pulp, and 36% reported symptoms related to canned peach. Canned peach and pulp symptoms were statistically associated, and symptoms to canned peach were significantly more frequently reported by patients with systemic symptoms. (83)
Interestingly, an Italian report on patients with peach-induced contact urticaria stated that these patients do not experience similar symptoms after handling botanically related fruit such as nectarines or other Rosaceae such as apple, pear, cherry or plum, suggesting possible differences in the surface layers of these fruits: freshly picked peaches are characterised by abundant surface fuzz, which is higher in lipid transfer protein. (52)
A study of the prevalence of allergy to various foods was conducted in the Netherlands. Individuals with tree pollen allergy were evaluated for skin-specific IgE, and the prevalence of sensitistion to apple, peach, and hazelnut was found to be 51 (64.6%), 61 (77.2%), and 71 (89.9%) patients, respectively. The concordance between serum-specific IgE and a case history for peach allergy was 71% in 79 consecutive patients with birch pollinosis. (81)
Oral allergy to peach is often associated with pollen allergy. A study reports on 7 patients with cypress pollen allergy, including symptoms during winter, who experienced oral allergy syndrome, urticaria or angioedema immediately following peach ingestion: 3 reported lip pruritus and oedema, 3 reported generalised urticaria, and 1 experienced angioedema. (74) In Spanish patients, every member of a group with pollinosis caused by grass or olive pollen, and with oral allergy symptoms after eating peach, had specific IgE antibodies to peach, and 4 out of 5 also to Bet v 2 (profilin). (46)
The relationship between pollen allergy and oral allergy syndrome to fruits and vegetables was evaluated in Sapporo, Japan. Of 843 patients with birch pollen (BP) allergy, 37% had episodes of oral allergy syndrome, and the rate of OAS combined with birch pollen allergy was higher than the rate of OAS combined with other allergies. The most common foods to cause OAS were apple, peach and cherry, followed by kiwi, pear, plum and melon. Birch pollen allergy patients demonstrated much more OAS with these foods than the patients without birch pollen allergy. (95)
In a Japanese study of 23 patients with Japanese cedar pollen allergy and OAS for fresh fruits and vegetables, the fruits that caused OAS included melon, apple, peach, and kiwi. Most patients with OAS exhibited hypersensitivity to more than 2 foods. Eleven of the 16 subjects with specific IgE antibodies for birch pollen did not suffer symptoms during the birch and alder pollen season. In those with specific IgE antibodies for fruit, 13 of 20 showed specific IgE for apple, and 17 had no specific IgE antibodies for melon; only 2 patients had specific IgE for kiwi fruit, and 1 for peach. (96)
A 32-year-old nurse with latex allergy experienced anaphylaxis following the ingestion of several members of the stone fruit family (i.e. plum, peach, and nectarine). A year before a recent anaphylactic episode following ingestion of plum, she had developed generalised pruritus, a sensation of a ‘thick’ tongue, and difficulty in swallowing and breathing following ingestion of a peach. She has eaten canned peach since that episode, without difficulty. Following this episode and one month prior to her hospitalisation for anaphylaxis to plum, she experienced anaphylaxis 30 minutes after eating a fresh nectarine. Presenting complaints included acute shortness of breath, a swollen tongue, and generalised pruritus. She was treated for anaphylaxis but six hours later developed a recurrence of tightness in her chest and throat. The patient had strongly positive skin tests to the freshly prepared fruit extracts, but serum specific IgE tests were equivocal or very low positive. In vitro latex-specific IgE tests were strongly positive. (97)
The allergenicity of peach is retained in the dried fruit. In a study of 102 children and adults with hypersensitivity to dried fruits, hypersensitivity to peach was detected in 47% of the cases. (79)
Allergic reactions to peach may occur to the hidden allergen in ice cream, or by indirect contact through kisses or utensils. (98)
A 28-year-old woman factory worker experienced occupational asthma and occupational rhinitis as a result of inhalation while handling peach. She also developed urticaria from ingesting peach. Bronchial challenge resulted in a 60% FEV1 fall within 10 minutes. (99) A study described a 21-year-old woman who developed primarily airborne sensitisation to lipid transfer protein of peach, and symptoms of severe perennial rhinitis 6 months after starting work in a wholesale fruit storehouse in Southern Italy where large amounts of fruit, including peaches, were handled. Symptoms subsided when she left the workplace for more than 5 days, and relapsed as soon as she was back at work. She subsequently developed severe food allergies to peach, hazelnut, peanut, apricot, plum and tomato. (100) Both instances may have resulted from the inhalation of lipid transfer protein, which is found in intact peach fuzz and may, in particular, result in respiratory allergy in fruit-store workers. (100)
The lipid transfer protein from peach, Pru p 3, has also been isolated from peach tree leaves and can act as a respiratory allergen and cause occupational rhinoconjunctivitis and asthma, as described in a fruit grower. In this case, skin-specific IgE was found for peach leaf and fruit. A specific bronchial provocation test with peach leaf was positive, with both an immediate and a delayed response. Peach leaf extract contained concentrations of Pru p 3 similar to those found in peach skin. Specific IgE immunodetection showed that the patient's sera reacted with Pru p 3, and with a single major band from the peach leaf extract that was fully inhibited by Pru p 3. The conclusion was that the lipid transfer protein Pru p 3 from peach leaves can act as a respiratory allergen and cause occupational rhinoconjunctivitis and asthma. (101)
Compiled by Dr Harris Steinman, email@example.com
- Lleonart R, Cisteró A, Carreira J, Batista A, Moscoso del Prado J. Food allergy: identification of the major IgE-binding component of peach (Prunus persica). Ann Allergy 1992;69(2):128-30.
- 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 1994;94(4):699-707.
- International Union of Immunological Societies Allergen Nomenclature: IUIS official list http://www.allergen.org/. Accessed November 2012.
- Gaier S, Marsh J, Oberhuber C, Rigby NM, Lovegrove A, Alessandri S, Briza P, Radauer C, Zuidmeer L, van Ree R, Hemmer W, Sancho AI, Mills C, Hoffmann-Sommergruber K, Shewry PR. Purification and structural stability of the peach allergens Pru p 1 and Pru p 3. Mol Nutr Food Res 2008;52(S2):S220-9.
- Ahrazem O, Jimeno L, López-Torrejón G, Herrero M, Espada JL, Sánchez-Monge R, Duffort O, Barber D, Salcedo G. Assessing allergen levels in peach and nectarine cultivars. Ann Allergy Asthma Immunol 2007;99(1):42-7.
- Brenna O, Pompei C, Ortolani C, Pravettoni V, Farioli L, Pastorello EA. Technological processes to decrease the allergenicity of peach juice and nectar. J Agric Food Chem 2000;48(2):493-7.
- Maeda N, Inomata N, Morita A, Kirino M, Moriyama T, Ikezawa Z. Anaphylaxis due to peach with negative ImmunoCAP result to peach allergens, including rPru p 1, rPru p 3, AND rPru p 4: A report of two cases. [Japanese] Arerugi 2009;58(2):140-7.
- Pastorello EA, Farioli L, Pravettoni V, Scibilia J, Mascheri A, Borgonovo L, Piantanida M, Primavesi L, Stafylaraki C, Pasqualetti S, Schroeder J, Nichelatti M, Marocchi A. Pru p 3-sensitised Italian peach-allergic patients are less likely to develop severe symptoms when also presenting IgE antibodies to Pru p 1 and Pru p 4. Int Arch Allergy Immunol 2011;156(4):362-72.
- Hwang EK, Kim JH, Nam YH, Jin HJ, Park HS. Diagnostic value of the allergen, Pru p 1 in adult patients with birch pollen-associated oral allergy syndrome. Allergy 2011;66(12):1621-2.
- Pasini G, Curioni A, Vegro M, Pagani M, Masi A, Schievano E, Antico A. Extraction and mass spectrometry identification of a major peach allergen Pru p 1. J Sci Food Agric 2011 Sep 14. [Epub ahead of print]
- Palacin A, Tordesillas L, Gamboa P, Sanchez-Monge R, Cuesta-Herranz J, Sanz ML, Barber D, Salcedo G, az-Perales A. Characterization of peach thaumatin-like proteins and their identification as major peach allergens. Clin Exp Allergy 2010;40(9):1422-30.
- Palacín A, Rivas LA, Gómez-Casado C, Aguirre J, Tordesillas L, Bartra J, Blanco C, Carrillo T, Cuesta-Herranz J, Bonny JA, Flores E, García-Alvarez-Eire MG, García-Nuñez I, Fernández FJ, Gamboa P, Muñoz R, et al. The involvement of thaumatin-like proteins in plant food cross-reactivity: a multicenter study using a specific protein microarray. PLoS One 2012;7(9):e44088.
- Dagar A, Friedman H, Lurie S. Thaumatin-like proteins and their possible role in protection against chilling injury in peach fruit. Postharv Biol Tec 2010;57(2):77-85.
- Chen L, Zhang S, Illa E, Song L, Wu S, Howad W, Arús P, van de Weg E, Chen K, Gao Z. Genomic characterization of putative allergen genes in peach/almond and their synteny with apple. BMC Genomics 2008;9:543.
- Pastorello EA, Ortolani C, Baroglio C, Pravettoni V, Ispano M, Giuffrida MG, Fortunato D, Farioli L, Monza M, Napolitano L, Sacco M, Scibola E, Conti A. Complete amino acid sequence determination of the major allergen of peach (Prunus persica) Pru p 1. Biol Chem 1999;380:1315-20.
- van Ree R, Fernandez-Rivas M, Cuevas M, van Wijngaarden M, Aalberse RC. Pollen-related allergy to peach and apple: an important role for profilin. J Allergy Clin Immunol 1995;95(3):726-34.
- Pastorello EA, Incorvaia C, Pravettoni V, Farioli L, Conti A, Vigano G, Rivolta F, Ispano M, Rotondo F, Ortolani C. New allergens in fruits and vegetables. Allergy 1998;53(46 Suppl):48-51.
- 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 2000;122(1):20-32.
- Sánchez-Monge R, Lombardero M, García-Sellés FJ, Barber D, Salcedo G. Lipid-transfer proteins are relevant allergens in fruit allergy. J Allergy Clin Immunol 1999;103(3 Pt 1):514-9.
- Diaz-Perales A, Garcia-Casado G, Sanchez-Monge R, Garcia-Selles FJ, Barber D, Salcedo G. cDNA cloning and heterologous expression of the major allergens from peach and apple belonging to the lipid-transfer protein family. Clin Exp Allergy 2002;32(1):87-92.
- Carnés J, Fernández-Caldas E, Gallego MT, Ferrer A, Cuesta-Herranz J. Pru p 3 (LTP) content in peach extracts. Allergy 2002;57(11):1071-5.
- Díaz-Perales A, Sanz ML, García-Casado G, Sánchez-Monge R, García-Selles FJ, Lombardero M, Polo F, Gamboa PM, Barber D, Salcedo G. Recombinant Pru p 3 and natural Pru p 3, a major peach allergen, show equivalent immunologic reactivity: a new tool for the diagnosis of fruit allergy. J Allergy Clin Immunol 2003;111(3):628-33.
- Duffort OA, Polo F, Lombardero M, Díaz-Perales A, Sánchez-Monge R, García-Casado G, Salcedo G, Barber D. Immunoassay to quantify the major peach allergen Pru p 3 in foodstuffs. Differential allergen release and stability under physiological conditions. J Agric Food Chem 2002;50(26):7738-41.
- Borges JP, Jauneau A, Brulé C, Culerrier R, Barre A, Didier A, Rougé P. The lipid transfer proteins (LTP) essentially concentrate in the skin of Rosaceae fruits as cell surface exposed allergens. Plant Physiol Biochem 2006;44(10):535-42.
- Pasquato N, Berni R, Folli C, Folloni S, Cianci M, Pantano S, Helliwell JR, Zanotti G. Crystal structure of peach Pru p 3, the prototypic member of the family of plant non-specific lipid transfer protein pan-allergens. J Mol Biol 2006;356(3):684-94.
- Zuidmeer L, van Leeuwen WA, Kleine B, Cornelissen J, Bulder I, Rafalska I, Tellez BN, Akkerdaas JH, Asero R, Fernandez RM, Gonzalez ME, van Ree RR. Lipid transfer proteins from fruit: cloning, expression and quantification. Int Arch Allergy Immunol 2005;137(4):273-81.
- Fernandez-Rivas M, Gonzalez-Mancebo E, Rodriguez-Perez R, Benito C, Sanchez-Monge R, Salcedo G, Alonso MD, Rosado A, Tejedor MA, Vila C, Casas ML. Clinically relevant peach allergy is related to peach lipid transfer protein, Pru p 3, in the Spanish population. J Allergy Clin Immunol 2003;112(4):789-95.
- Pastorello EA, Farioli L, Pravettoni V, Ortolani C, Ispano M, Monza M, Baroglio C, Scibola E, Ansaloni R, Incorvaia C, Conti A. The major allergen of peach (Prunus persica) is a lipid transfer protein. J Allergy Clin Immunol 1999;103(3 Pt 1):520-6.
- Borges JP, Barre A, Culerrier R, Granier C, Didier A, Rougé P. Lipid transfer proteins from Rosaceae fruits share consensus epitopes responsible for their IgE-binding cross-reactivity. Biochem Biophys Res Commun 2008;365(4):685-90.
- Pacios LF, Tordesillas L, Cuesta-Herranz J, Compes E, Sánchez-Monge R, Palacín A, Salcedo G, Díaz-Perales A. Mimotope mapping as a complementary strategy to define allergen IgE-epitopes: Peach Pru p 3 allergen as a model. Mol Immunol 2008;45(8):2269-76.
- Lauer I, Miguel-Moncin MS, Abel T, Foetisch K, Hartz C, Fortunato D, Cistero-Bahima A, Vieths S, Scheurer S. Identification of a plane pollen lipid transfer protein (Pla a 3) and its immunological relation to the peach lipid-transfer protein, Pru p 3. Clin Exp Allergy 2007;37(2):261-9.
- Gamboa PM, Cáceres O, Antepara I, Sánchez-Monge R, Ahrazem O, Salcedo G, Barber D, Lombardero M, Sanz ML. Two different profiles of peach allergy in the north of Spain. Allergy 2007;62(4):408-14.
- Garino C, Zitelli F, Travaglia F, Colsson JD, Cravotto G, Arlorio M. Evaluation of the impact of sequential microwave/ultrasound processing on the IgE binding properties of Pru p 3 in treated peach juice. J Agric Food Chem 2012;60(35):8755-62.
- Novembre E, Mori F, Contestabile S, Rossi ME, Pucci N. Correlation of anti-pru p 3 IgE levels with severity of peach allergy reactions in children. Ann Allergy Asthma Immunol 2012;108(4):271-4.
- Cavatorta V, Sforza S, Aquino G, Galaverna G, Dossena A, Pastorello EA, Marchelli R. In vitro gastrointestinal digestion of the major peach allergen Pru p 3, a lipid transfer protein: molecular characterization of the products and assessment of their IgE binding abilities. Mol Nutr Food Res 2010;54(10):1452-7.
- Toda M, Reese G, Gadermaier G, Schulten V, Lauer I, Egger M, Briza P, Randow S, Wolfheimer S, Kigongo V, Del Mar San Miguel Moncin M, Fötisch K, Bohle B, Vieths S, Scheurer S. Protein unfolding strongly modulates the allergenicity and immunogenicity of Pru p 3, the major peach allergen. J Allergy Clin Immunol 2011;128(5):1022-30.e1-7.
- Schulten V, Nagl B, Scala E, Bernardi ML, Mari A, Ciardiello MA, Lauer I, Scheurer S, Briza P, Jurets A, Ferreira F, Jahn-Schmid B, Fischer GF, Bohle B. Pru p 3, the nonspecific lipid transfer protein from peach, dominates the immune response to its homolog in hazelnut. Allergy 2011;66(8):1005-13.
- Asero R. Co-recognition of lipid transfer protein in pollen and foods in northern Italy: clinician's view. Eur Ann Allergy Clin Immunol 2010;42(6):205-8.
- Pastorello EA, Monza M, Pravettoni V, Longhi R, Bonara P, Scibilia J, Primavesi L, Scorza R. Characterization of the T-cell epitopes of the major peach allergen Pru p 3. Int Arch Allergy Immunol 2010;153(1):1-12.
- Hartz C, Lauer I, del Mar San Miguel Moncin M, Cistero-Bahima A, Foetisch K, Lidholm J, Vieths S, Scheurer S. Comparison of IgE-binding capacity, cross-reactivity and biological potency of allergenic non-specific lipid transfer proteins from peach, cherry and hazelnut. Int Arch Allergy Immunol 2010;153(4):335-46.
- Asakura K, Yamamoto T, Shirasaki H, Honma T. evaluation of relationships between foods and pollen antigens in peach oral allergy patients -serous specific IgE levels of peach recombinant antigen-.[Japanese] Arerugi 2009;58(2):133-9.
- Rossi RE, Monasterolo G, Canonica GW, Passalacqua G. Systemic reactions to peach are associated with high levels of specific IgE to Pru p 3. Allergy 2009;64(12):1795-6.
- Gaier S, Oberhuber C, Hemmer W, Radauer C, Rigby NM, Marsh JT, Mills CE, Shewry PR, Hoffmann-Sommergruber K. Pru p 3 as a marker for symptom severity for patients with peach allergy in a birch pollen environment. J Allergy Clin Immunol 2009;124(1):166-7.
- Tordesillas L, Cuesta-Herranz J, Gonzalez-Muñoz M, Pacios LF, Compés E, Garcia-Carrasco B, Sanchez-Monge R, Salcedo G, Diaz-Perales A. T-cell epitopes of the major peach allergen, Pru p 3: Identification and differential T-cell response of peach-allergic and non-allergic subjects. Mol Immunol 2009;46(4):722-8.
- Cavatorta V, Sforza S, Mastrobuoni G, Pieraccini G, Francese S, Moneti G, Dossena A, Pastorello EA, Marchelli R. Unambiguous characterization and tissue localization of Pru P 3 peach allergen by electrospray mass spectrometry and MALDI imaging. J Mass Spectrom 2009;44(6):891-7.
- Daschner A, Crespo JF, Pascual CY. Specific IgE to recombinant vegetal panallergen (rBet v 2) and fruit allergy in pollinic patients. Allergy 1998;53(6):614-8.
- Rodríguez-Perez R, Fernández-Rivas M, González-Mancebo E, Sánchez-Monge R, Díaz-Perales A, Salcedo G. Peach profilin: cloning, heterologous expression and cross-reactivity with Bet v 2. Allergy 2003;58(7):635-40.
- Tuppo L, Alessandri C, Pomponi D, Picone D, Tamburrini M, Ferrara R, Petriccione M, Mangone I, Palazzo P, Liso M, Giangrieco I, Crescenzo R, Bernardi ML, Zennaro D, Helmer-Citterich M, Mari A, Ciardiello MA. Peamaclein - A new peach allergenic protein: similarities, differences and misleading features compared to Pru p 3. Clin Exp Allergy 2012 doi: 10.1111/cea.12028.
- Barral P, Batanero E, Palomares O, Quiralte J, Villalba M, Rodríguez R. A major allergen from pollen defines a novel family of plant proteins and shows intra- and interspecies [correction of interspecie] cross-reactivity. J Immunol 2004;172(6):3644-51.
- Thimmapuram J, Ko TS, Korban SS. Characterization and expression of beta-1,3-glucanase genes in peach. Mol Genet Genomics 2001;265(3):469-79.
- Zuidmeer L, van RR R. Lipid transfer protein allergy: primary food allergy or pollen/food syndrome in some cases. Curr Opin Allergy Clin Immunol 2007;7(3):269-73.
- Asero R, Mistrello G, Amato S, Roncarolo D, Martinelli A, Zaccarini M. Peach fuzz contains large amounts of lipid transfer protein: is this the cause of the high prevalence of sensitization to LTP in Mediterranean countries? Allerg Immunol (Paris) 2006;38(4):118-21.
- Brenna OV, Pastorello EA, Farioli L, Pravettoni V, Pompei C. Presence of allergenic proteins in different peach (Prunus persica) cultivars and dependence of their content on fruit ripening. J Agric Food Chem 2004;52(26):7997-8000.
- Sankian M, Varasteh A, Pazouki N, Mahmoudi M. Sequence homology: A poor predictive value for profilins cross-reactivity. Clin Mol Allergy 2005;3(1):13.
- 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 2000;106(1 Pt 1):183-9.
- Scheurer S, Pastorello EA, Wangorsch A, Kastner M, Haustein D, Vieths S. Recombinant allergens Pru av 1 and Pru av 4 and a newly identified lipid transfer protein in the in vitro diagnosis of cherry allergy. J Allergy Clin Immunol 2001;107(4):724-31.
- Sanchez-Monge R, Blanco C, Lopez-Torrejon G, Cumplido J, Recas M, Figueroa J, Carrillo T, Salcedo G. Differential allergen sensitization patterns in chestnut allergy with or without associated latex-fruit syndrome. J Allergy Clin Immunol 2006;118(3):705-10.
- Palacin A, Cumplido J, Figueroa J, Ahrazem O, Sanchez-Monge R, Carrillo T, Salcedo G, Blanco C. Cabbage lipid transfer protein Bra o 3 is a major allergen responsible for cross-reactivity between plant foods and pollens. J Allergy Clin Immunol 2006;117(6):1423-9.
- Pastorello EA, Farioli L, Pravettoni V, Robino AM, Scibilia J, Fortunato D, Conti A, Borgonovo L, Bengtsson A, Ortolani C. Lipid transfer protein and vicilin are important walnut allergens in patients not allergic to pollen. J Allergy Clin Immunol 2004;114(4):908-14.
- San Miguel-Moncin M, Krail M, Scheurer S, Enrique E, Alonso R, Conti A, Cistero-Bahima A, Vieths S. Lettuce anaphylaxis: identification of a lipid transfer protein as the major allergen. Allergy 2003;58(6):511-7.
- Pastorello EA, Vieths S, Pravettoni V, Farioli L, Trambaioli C, Fortunato D, Lüttkopf D, Calamari M, Ansaloni R, Scibilia J, Ballmer-Weber BK, Poulsen LK, Wütrich B, Hansen KS, Robino AM, Ortolani C, Conti A. Identification of hazelnut major allergens in sensitive patients with positive double-blind, placebo-controlled food challenge results. J Allergy Clin Immunol 2002;109(3):563-70.
- Pastorello EA, Farioli L, Pravettoni V, Ortolani C, Fortunato D, Giuffrida MG, Perono Garoffo L, Calamari AM, Brenna O, Conti A. Identification of grape and wine allergens as an endochitinase 4, a lipid-transfer protein, and a thaumatin. J Allergy Clin Immunol 2003;111(2):350-9.
- Asero R, Mistrello G, Roncarolo D, Amato S, van Ree R. A case of allergy to beer showing cross-reactivity between lipid transfer proteins. Ann Allergy Asthma Immunol 2001;87(1):65-7.
- Asero R, Mistrello G, Roncarolo D, Amato S. Relationship between peach lipid transfer protein specific IgE levels and hypersensitivity to non-Rosaceae vegetable foods in patients allergic to lipid transfer protein. Ann Allergy Asthma Immunol 2004;92(2):268-72.
- Egger M, Mutschlechner S, Wopfner N, Gadermaier G, Briza P, Ferreira F. Pollen-food syndromes associated with weed pollinosis: an update from the molecular point of view. Allergy 2006;61(4):461-76.
- Lombardero M, Garcia-Selles FJ, Polo F, Jimeno L, Chamorro MJ, Garcia-Casado G, Sanchez-Monge R, Diaz-Perales A, Salcedo G, Barber D. Prevalence of sensitization to Artemisia allergens Art v 1, Art v 3 and Art v 60 kDa. Cross-reactivity among Art v 3 and other relevant lipid-transfer protein allergens. Clin Exp Allergy 2004;34(9):1415-21.
- Pastorello EA, Pravettoni V, Farioli L, Rivolta F, Conti A, Ispano M, Fortunato D, Bengtsson A, Bianchi M. Hypersensitivity to mugwort (Artemisia vulgaris) in patients with peach allergy is due to a common lipid transfer protein allergen and is often without clinical expression. J Allergy Clin Immunol 2002;110(2 Pt 1):310-7.
- García-Sellés FJ, Díaz-Perales A, Sánchez-Monge R, Alcántara M, Lombardero M, Barber D, Salcedo G, Fernández-Rivas M. Patterns of reactivity to lipid transfer proteins of plant foods and Artemisia pollen: an in vivo study.: An in vivo Study. Int Arch Allergy Immunol 2002;128(2):115-22.
- Salcedo G, Sánchez-Monge R, Barber D, Díaz-Perales A. Plant non-specific lipid transfer proteins: an interface between plant defence and human allergy. Biochim Biophys Acta 2007;1771(6):781-91.
- Cuesta-Herranz J, Lázaro M, Martínez A, Figueredo E, Palacios R, de-Las-Heras M, Martínez J. Pollen allergy in peach-allergic patients: sensitization and cross-reactivity to taxonomically unrelated pollens. J Allergy Clin Immunol 1999;104(3 Pt 1):688-94.
- Wensing M, Akkerdaas JH, Van Leeuwen WA, Stapel SO, Bruijnzeel-Koomen CA, Aalberse RC, Bast BJ, Knulst AC, Van Ree R. IgE to Bet v 1 and profilin: Cross-reactivity patterns and clinical relevance. J Allergy Clin Immunol 2002;110(3):435-42.
- Brehler R, Theissen U, Mohr C, Luger T. "Latex-fruit syndrome": frequency of cross-reacting IgE antibodies. Allergy 1997;52(4):404-10.
- Garcia Ortiz JC, Moyano JC, Alvarez M, Bellido J. Latex allergy in fruit-allergic patients. Allergy 1998;53(5):532-6.
- Hugues B, Didierlaurent A, Charpin D. Cross-reactivity between cypress pollen and peach: a report of seven cases. Allergy 2006;61(10):1241-3.
- Gotoda H, Maguchi S, Kawahara H, Terayama Y, Fukuda S. Springtime pollinosis and oral allergy syndrome in Sapporo. Auris Nasus Larynx 2001;28 Suppl:S49-52.
- Bircher AJ, Van Melle G, Haller E, Curty B, Frei PC. IgE to food allergens are highly prevalent in patients allergic to pollens, with and without symptoms of food allergy. Clin Exp Allergy 1994;24(4):367-74.
- Marzban G, Herndl A, Kolarich D, Maghuly F, Mansfeld A, Hemmer W, Katinger H, Laimer M. Identification of four IgE-reactive proteins in raspberry (Rubus ideaeus L.). Mol Nutr Food Res 2008;52(12):1497-506.
- Ortolani C, Ispano M, Pastorello E, Bigi A, Ansaloni R. The oral allergy syndrome. Ann Allergy 1988;61(6 Pt 2):47-52.
- Amat Par P, Sanosa Valls J, Lluch Perez M, Malet Casajuana A, Garcia Calderon PA. Dried fruit hypersensitivity and its correlation with pollen allergy. Allergol Immunopathol (Madr) 1990;18(1):27-34.
- Eriksson NE. Food sensitivity reported by patients with asthma and hay fever. A relationship between food sensitivity and birch pollen-allergy and between food sensitivity and acetylsalicylic acid intolerance. Allergy 1978;33(4):189-96.
- de Groot H, de Jong NW, Vuijk MH, Gerth van Wijk R. Birch pollinosis and atopy caused by apple, peach, and hazelnut; comparison of three extraction procedures with two apple strains. Allergy 1996;51(10):712-8.
- Guillet MH, Guillet G. Food urticaria in children. Review of 51 cases. [French]. Allerg Immunol (Paris) 1993;25(8):333-8.
- Cuesta-Herranz J, Lázaro M, de las Heras M, Lluch M, Figueredo E, Umpierrez A, Hernandez J, Cuesta C. Peach allergy pattern: experience in 70 patients. Allergy 1998;53(1):78-82.
- Kivity S, Dunner K, Marian Y. The pattern of food hypersensitivity in patients with onset after 10 years of age. Clin Exp Allergy 1994;24(1):19-22.
- Crespo JF, Rodriguez J, James JM, Daroca P, Reano M, Vives R. Reactivity to potential cross-reactive foods in fruit-allergic patients: implications for prescribing food avoidance. Allergy 2002;57(10):946-9.
- Malet A, Sanosa J, García-Calderón PA. Diagnosis of allergy to peach. A comparative study of "in vivo" and "in vitro" techniques. Allergol Immunopathol (Madr) 1988;16(3):181-4.
- Zuidmeer L, Goldhahn K, Rona RJ, Gislason D, Madsen C, Summers C, Sodergren E, Dahlstrom J, Lindner T, Sigurdardottir ST, McBride D, Keil T. The prevalence of plant food allergies: a systematic review. J Allergy Clin Immunol 2008;121(5):1210-8.
- Ono E, Maeda Y, Tanimoto H, Fukutomi Y, Oshikata C, Sekiya K, Tuburai T, Turikisawa N, Otomo M, Taniguchi M, Ishii H, Asahina A, Miyazaki E, Kumamoto T, Akiyama K. Clinical features of oral allergy syndrome to plant foods allergens in Kanto regions. [Japanese] Arerugi 2007;56(6):587-92.
- Yamamoto T, Asakura K, Shirasaki H, Himi T. Clustering of food causing oral allergy syndrome in patients with birch pollen allergy. [Japanese] Nippon Jibiinkoka Gakkai Kaiho 2008;111(8):588-93.
- Fernandez Rivas M, van Ree R, Cuevas M. Allergy to Rosaceae fruits without related pollinosis. J Allergy Clin Immunol 1997;100(6 Pt 1):728-33.
- Hartz C, San Miguel-Moncin MM, Cistero-Bahima A, Fotisch K, Metzner KJ, Fortunato D, Lidholm J, Vieths S, Scheurer S. Molecular characterisation of Lac s 1, the major allergen from lettuce (Lactuca sativa). Mol Immunol 2007;44(11):2820-30.
- Pajno GB, Passalacqua G, La Grutta S, Vita D, Feliciotto R, Parmiani S, Barberio G. True multifood allergy in a 4-year-old child: a case study. Allergol Immunopathol (Madr) 2002;30(6):338-41.
- Ellis AK, Day JH. Incidence and characteristics of biphasic anaphylaxis: a prospective evaluation of 103 patients. Ann Allergy Asthma Immunol 2007;98(1):64-9.
- Lombardi P, Campolmi P, Giorgini S, Spallanzani P, Sertoli A. Contact Urticaria from fish, honey and peach skin. Contact Dermatitis 1983;9:422-3.
- Yamamoto T, Asakura K, Shirasaki H, Himi T, Ogasawara H, Narita S, Kataura A Relationship between pollen allergy and oral allergy syndrome. Nippon Jibiinkoka Gakkai Kaiho 2005;108(10):971-9.
- Ishida T, Murai K, Yasuda T, Satou T, Sejima T, Kitamura K. Oral allergy syndrome in patients with Japanese cedar pollinosis. [Japanese] Nippon Jibiinkoka Gakkai Kaiho 2000;103(3):199-205.
- Weiss SJ, Halsey JF. A nurse with anaphylaxis to stone fruits and latex sensitivity: potential diagnostic difficulties to consider. Ann Allergy Asthma Immunol 1996;77(6):504-8.
- Anibarro B, Seoane FJ, Mugica MV. Involvement of hidden allergens in food allergic reactions. J Investig Allergol Clin Immunol 2007;17(3):168-72.
- Carrasquer Moya C, Pelaez Hernandez A, Dura Calatayud M, Burches Baixauli E, Berto Salom JM, Sastre Sastre A. Allergy to peach. Allergy 2002;57(8):756-7.
- Borghesan F, Mistrello G, Roncarolo D, Amato S, Plebani M, Asero R. Respiratory allergy to lipid transfer protein. Int Arch Allergy Immunol 2008;147(2):161-5.
- Garcia B, Lombardero M, Echechipia S, Olaguibel J, Diaz-Perales A, Sanchez-Monge R, Barber D, Salcedo G, Tabar A. Respiratory allergy to peach leaves and lipid-transfer proteins. Clin Exp Allergy 2004;34(2):291-5.