Tomato is eaten raw in salads or cooked as a vegetable and is a frequent ingredient in soups and stews. It is found in most pizzas. Tomato is used in sauces, pickles and chutney, which is often made from green tomato.
Oral Allergy Syndrome (OAS), neurodermatitis, urticaria, nausea and anaphylaxis (Westphal et al. 2004) [918]
Urticaria/angioedema, dermatitis, oral allergy syndrome, rhinitis, and abdominal pain (Zacharisen et al. 2002) [922]
Reche et al. (2001) [927] studied a group (A) of 30 non-latex-allergic patients, and a group (B) of 10 latex-allergic patients. In group A, the most frequent clinical symptom with tomato was oral allergy syndrome (OAS), although urticaria was the most frequent symptom in group B. In this group, anaphylaxis occurred in 20% of the patients.
Positive reactions to tomato (39.2%) were observed in children with allergy to grass pollen. In children with positive skin test to tomato a 45% correlation with a positive RAST result were observed (de Martino et al. 1988) [950]
Fresh tomato extracts prepared from the skin, seeds, and flesh of red, ripe tomatoes (Zacharisen et al. 2002) [922]
Commercial tomato extract (Foetisch et al. 2001) [928]
Tomato extract. To prepare this extract tomato pericarp was dissected and homogenized for 15 s in cold distilled water. After centrifugation at 2400 g for 10 min, the pellet was collected and resuspended in 1 m NaCl at pH 6 with 1 m NaOH. After stirring for 3 h at 4 °C, the debris was removed by centrifugation at 2400 g for 10 min. The supernatant was filtered and brought to 75% saturation with ammonium sulphate for 18 h. The precipitate was collected by centrifugation at 10 000 g for 20 min and suspended in 0.15 m NaCl (pH 6). This extract was dialysed against 0.15 m NaCl (pH 6) at 4 °C over two nights. The residues were removed by centrifugation at 10 000 g for 20 min. (Kondo et al. 2002 [949])
Commercial tomato extract and recombinant Lyc e 1 (Westphal et al. 2004) [918]
Tomato extract. To prepare the extract 200 g of ripe tomato was washed, ground, and soaked for 1 h in 500 ml of PBS with 10 mM ascorbic acid as an antioxidant. The mixture was stirred for 2 h at 4°C and centrifuged at 7000 g for 40 min at 4°C. The supernatant was dialyzed (molecular weight cutoff: >3500 Da) at 4°C for 24 h against glycine, centrifuged at 15 000 g for 30 min at 4°C, and filtered through a 0.45-µm filter. The material was lyophilized. (Reche et al. 2001) [927]
ELISA and RAST (Zacharisen et al. 2002) [922]
CAP-FEIA (Reche et al. 2001) [927]
RAST (Kondo et al. 2002) [949]
CAP, EAST, EAST inhibition and CCD (crossreactive carbohydrate determinants)-ELISA (Foetish et al. 2001) [928]
ELISA, EAST, CAP-FEIA, histamine release (Westphal et al. 2004) [918]
Two patients with adverse symptoms after ingesting tomato (Zacharisen et al. 2002) [922]
Forty patients with a history of adverse reactions to tomato. The patients were divided into two groups; group A comprising 30 non-latex-allergic patients, and group B comprising 10 patients with latex allergy (Reche et al. 2001) [927]
Five individuals with OAS after eating fresh tomatoes. (Kondo et al. 2002) [949]
32 pollen-allergic patients with a history of adverse reactions to tomato (Foetisch et al. 2001) [928]
50 patients with a positive case history of immediate type reactions to tomato fruit (Westphal et al. 2004) [918]
RAST assays were positive to tomato in both patients (Zacharisen et al. 2002) [922]
All patients showed specific IgE to tomato (Reche et al. 2001) [927]
In RAST inhibition assays, the IgE binding from the sera from four out of five subjects with allergy to Japanese cedar pollen was inhibited by more than 50% by tomato fruit extracts. The IgE binding to tomato fruit was inhibited more than 50% by Japanese cedar pollen extracts in 3/5 sera. (Kondo et al. 2002) [949]
Tomato allergy was found to occur with a prevalence of about 9% in a group of birch pollen-allergic patients. Of the patients with adverse reactions to tomato, 44% presented IgE to tomato profilin and 35.5% specific IgE to CCD. Two patients were sensitized to a lipid transfer protein in tomato (Foetisch et al. 2001) [928]
Recombinant tomato profilin induced histamine release from human basophils in a range of 18-40% in a dose-dependent manner. Histamine release of up to 30% or 55% was obtained with the highest concentration of tomato extract. In the ELISA assays, 11 of 50 patients (22%) reacted with the purified recombinant tomato profilin (Westphal et al. 2004) [918]
Tomato protein extract was separated on either 12% or 7.5-20% polyacrylamide gels under reducing conditions (Willerroider et al. 2003) [914]
Proteins were separated by sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS-PAGE) under reducing conditions (Westphal et al. 2003) [919]
SDS-PAGE was performed with a 12% polyacrylamide separating gel and a stacking gel of 4% (Recher et al. 2001) [927]
Sodium dodecylsulphate-polyacrylamide gel electrophoresis was performed in a 16% Tris-glycine precast gel under reducing conditions (Kondo et al. 2002) [949]
Proteins were separated by 2D-gel electrophoresis (Foetisch et al. 2001) [928]
The proteins were transferred onto nitrocellulose membranes. The membrane was incubated with patient sera (1:4). Bound IgE was detected by 125I-labelled anti-human IgE antibodies(1:20) and visualised by autoradiography (Willerroider et al. 2003) [914]
For immunoblot analysis, proteins were transferred onto 0.45 µm nitrocellulose membranes by tank blotting and membrane was blocked in TBS/0.3% (v/v) Tween-20. After incubation with 1 : 10 diluted patients' sera, immunostaining of bound IgE antibodies was performed with an alkaline phosphatase conjugated anti-human-IgE antibody (1 : 750 dilution) and the developed with an alkaline phosphatase conjugate substrate kit (Westphal et al. 2003) [919]
Proteins were electrophoretically transferred to a PDVF membrane using a minitransfer chamber. Blots were incubated with pool sera diluted 1:1. Alkaline-phosphatase-conjugated goat anti-human IgE (1:2000) was added and incubated. The blot was developed with an alkaline-phosphatase-conjugate substrate kit of nitroblue tetrazolium and 5-bromo-4-chloro-3 indolyl-phosphatase (Recher et al. 2001) [927]
Proteins were transferred to Immobilon™ -P Membranes. For detection of bound IgE, a phosphatase-labelled goat anti-human IgE antibody diluted 1 : 2000 was used and developed with BCIP/NBT solution (Kondo et al. 2002) [949]
Proteins were transferred to PVDF membranes (Foetisch et al. 2001) [928]
All the patients (11) displayed IgE binding to the 14 kDa protein (profilin) from the extract (Willerroider et al. 2003) [914]
Out of 49 sera from German patients with tomato-related symptoms 18 (37%) recognized several bands above 20 kDa. From the Spanish group, 10 out of 29 (34.5%) sera showed reactivity in the high molecular mass range. The authors also detected binding to proteins with a molecular mass of 15 and 9 kDa (Westphal et al. 2003) [919]
Group A of patients reacted to a double protein band at 44 and 46 kDa, a triple band at 67 kDa, several proteins at 20 and 30 kDa; and a protein between 14 and 20 kDa. In pool B, the profile obtained was similar to pool A, except that it had two more bands at 14 and 17 kDa (Reche et al. 2001) [927]
The IgE binding to some protein bands from both Japanese cedar pollen and tomato fruit extracts are mutually inhibited, but the protein bands involved in this cross-reactivity differed between patients (Kondo et al. 2002) [949]
One patient reacted specifically to a 43-kDa protein band on IgE immunoblot (Zacharisen et al. 2002) [922]
Foetisch et al. (2001) [928] revealed beta -fructofuranosidase, polygalacturonase 2A, and pectinesterase as further tomato allergens.
Cross-reactivity to peanut and grass pollen has been observed by RAST inhibition assays (de Martino et al. 1988) [950] and by EAST inhibition assay (Petersen et al. 1996) [161].
By RAST-inhibition, cross-reactivity among latex, avocado, chestnut, and banana was demonstrated by Blanco et al. (1994) [288]
Cross-reactivity has been observed between cedar pollen (Cryptomeria japonica) by RAST inhibition assays (Kondo et al. 1997 and 2002) [924] [949]. Cross-reactivity between tomato, potato and latex by RAST inhibition assays has been described by Reche et al. (2001) [927]
Kondo et al. (2001) [920] identified the proteins in tomato recognised by sera from patients with food allergy and OAS to tomato. These proteins were polygalacturonase 2A (46 kDa), beta-fructofuranosidase (22 kDa), superoxide dismutase (18 kDa) and pectinesterase (14 kDa).
A protein with a molecular mass of 45kDa was strongly recognised by 67 % of the allergic patients (Weangsripanaval et al. 2003) [921]
Profilin, Pfam PF00235
Q8VWR0:Swissprot: http://ca.expasy.org/cgi-bin/niceprot.pl?Q8VWR0
AY061819; EMBL
Q93YG7:Swissprot: http://us.expasy.org/cgi-bin/niceprot.pl?Q93YG7
AJ417553 EMBL
14080 kDa (Westphal et al. 2004) [918]
14257 kDa (Willerroider et al. 2003) [914]
There are only few studies on the stability of profilins most of them on celery profilin. Compared to other allergens, profilin is a moderately stable protein, more resistant than Bet v 1 homologues but less stable than lipid transfer proteins or corss-reactive carbohydrate deteminants of glycoporein allergens.
Purified rLyc e 1completely abolished the IgE binding to rCap a 2 (bell pepper profilin)(Willerroider et al. 2003) [914]
Western blotting performed by Petersen et al (1996) showed that profilin contributes considerably to the IgE cross-reactivity between tomato fruit and grass pollen.
Western blotting assays and ELISA inhibition experiments showed cross-reactivity with birch (Bet v 2) and celery (Api g 4) profilins (Westphal et al. 2004) [918]
pI 4.71(Westphal et al. 2004) [918]. pI 4.46 (Willerroider et al. 2003) [914]
Different profilin isoforms are thought to be present in tomato fruit (Westphal et al. 2004) [918]
Lyc e 1 sequence shows a high degree of identity (76-86%) to other plant profilins such as cherry (Pru av 4), pineapple (Ana c 1), banana (Mus xp 1), carrot (Dau c 4), celery (Api g 4) and birch (Bet v 2). Bell pepper showed the highest identity (91%) (Westphal et al. 2004) [918]; (Willerroider et al. 2003) [914]).
Lyc e 1 is found predominantly as dimers in solution, which can be reduced to monomers, with higher IgE binding capacity (Willerroider et al. 2003) [914]
Glycosyl hydrolases family 32, Pfam, PF00251
Q8RVW4:Swissprot:http://ca.expasy.org/cgi-bin/niceprot.pl?Q8RVW4
AF465613; AAL75450.1; - EMBL
Two isoforms, D11350; S70040 GenBank
Lyc e 2 has been purified from lyophilized tomato extract by hydrophobic interaction chromatography and gel chromatography (Westphal et al. 2003) [919]. The same authors have cloned and expressed the cDNA of two different isoforms of the protein, Lyc e 2.01 and Lyc e 2.02 in E. coli. The recombinant proteins were purified by electroelution and refolded.
The University of Manchester is not responsible for the content of external internet sites.
