Allergy information for: Lettuce (

Lactuca sativa (Garden lettuce)

)

Clinical History

• Number of Studies:1-5
• Number of Patients:11-20
• Symptoms:Anaphylaxis, pruritus of the oral cavity, urticaria-angioedema and gastric disorders (San Miguel-Moncin et al. 2003) [821]. Generalized pruritic, papular and erythematous eruption, associating facial and lingual oedema with tightness to throat (Vila et al. 1998) [823]. Dyspepsia and diarrhea (Helbling et al. 1994) [868]

Skin Prick Test

• Number of Studies:1-5
• Food/Type of allergen:

  Extracts and fresh lettuce (stalk and leaves) (Vila et al. 1998) [823]

  Commercial extracts and fresh lettuce leaf (San Miguel-Moncin et al. 2003) [821]

• Protocol: (controls, definition of positive etc)

  SPT was performed using the prick-prick technique. Histamine hydrochloride 10 ng/ml and saline solution 0.9% served as positive and negative controls, respectively. The reactions were read after 15 min and were considered to be positive if the diameter of the weal was 3 mm greater than the negative control. Histamine release test was also performed and considered positive if greater than 10% (Vila et al. 1998) [823]

  SPT was performed using the prick-prick technique. Histamine dihydrochloride 10 mg/ml and phosphate-buffered saline (PBS) solution served as positive and negative controls, respectively. The SPT was considered positive if the wheal area was 3 mm greater than the negative control, 15 min after testing (San Miguel-Moncin et al. 2003) [821]

• Number of Patients:

  1 patient diagnosed of seasonal asthma and rhinitis with sensitization to mugwort pollen, as well as food allergy with sensitization to peanut, peach and apple. After ingestion of lettuce she presented generalized, pruritic, papular and erythematous eruption, associating facial and lingual oedema with tightness to throat (Vila et al. 1998) [823]

  A 32-year-old man with a digestive and respiratory form of food allergy to lettuce and pollinosis (Franck et al. 1999) [822]

  14 patients with documented allergic reactions following lettuce ingestion (San Miguel-Moncin et al. 2003) [821]

• Summary of Results:

  SPT was positive for the extract and fresh lettuce. The histamine release test was positive, with a specific histamine release to lettuce of 59% (Vila et al. 1998) [823]

  The prick test was positive for lettuce (3.5 mm) against a 9% codeine control at 3 mm (Franck et al. 1999) [822]

  All patients were sensitized to Platanus pollen and suffered from pollinosis. Several patients were also sensitized to other pollens such as mugwort (50%), Parietaria (21%), and grass (14%). All patients were positive to lettuce both in SPT with commercial extract and with the fresh food. Most of the patients were sensitized to other plant-derived foods, and several of the foods causing a positive SPT were not tolerated by the patients, mainly hazelnut (57%) and peach (43%) (San Miguel-Moncin et al. 2003) [821]

IgE assay (by RAST, CAP etc)

• Number of Studies:0
• Food/Type of allergen:Lettuce extracts
• IgE protocol:

  Phadebas RAST and RAST inhibition (Helbling et al. 1994) [868]

  CAP-FEIA (Vila et al. 1998) [823]

  CAP RAST (Franck et al. 1999) [822]

  CAP RAST and/or EAST (San Miguel-Morcin et al. 2003) [821]

• Number of Patients:

  Three ragweed pollen allergic patients. Two had allergic reactions following lettuce ingestion and the third subject was skin-test positive to lettuce (Helbling et al. 1994) [868]

  A 26-year-old woman (Vila et al. 1998) [823]

  A 32-year-old man with a digestive and respiratory form of food allergy to lettuce and pollinosis (Franck et al. 1999) [822]

  14 patients with documented allergic reactions following lettuce ingestion (san Miguel-Moncin et al. 2003) [821]

• Summary of Results:

  All the patients were IgE positive (Helbling et al. 1994) [868]

  Vila et al. 1998 [823] determined a total IgE of 69.0 kU/L and a serum specific IgE to lettuce of 4.08 kU/L.

  Screening for specific IgE was negative (Franck et al. 1999) [822].

  12/14 patients had positive specific IgE to lettuce (San Miguel-Morcin et al. 2003) [821]

Immunoblotting

• Immunoblotting separation:

  Electrophoresis was performed on 8-25 % polyacrylamide gel. (Franck et al. 1999) [822].

  Electrophoresis was performed on 15%T/2.7C separation gels and 4%T/2.7C stacking gels under reducing conditions (Helbling et al. 1994) 868]

  Lettuce extract was separated under nonreducing conditions by Tricine-SDS-PAGE using a 16% T, 2.6% C separating gel overlaid by a 4% T, 2.6% C stacking gel (San Miguel-Moncin et al. 2003) [821]

  SDS-PAGE was carried out using 12.5% and 3% polyacrylamide gels under reducing conditions (Vila et al. 1998) [823]

• Immunoblotting detection method:

  Western blot was performed on a nitrocellulose membrane. The membrane was saturated in a 5% bovine serum albumin buffer, and then incubated with a 1:10 dilution of the patient's serum. The fixed IgE was observed by chemiluminescence using anti-IgE secondary antibodies, marked with peroxidase diluted 1:1000 in 1% BSA-0.1% PBS Tween buffer. After washing, the membrane was submerged in Luminol (Covalab) with H₂O₂. (Franck et al. 1999) [822]

  Western blot was performed on a nitrocellulose membrane (0.2 µm pore size). The membrane was saturated in a 1% bovine serum albumin buffer, and then incubated with a 1:2 dilution of the patient's serum. The fixed IgE was observed with radiolabeled anti-IgE and developed using X-ray film (Helbling et al. 1994) [868]

  Proteins were transferred onto a 0.2 µm nitrocellulose membrane by tank blotting. For the detection of allergen-specific IgE antibodies sera were diluted 1:5 and incubated with the blot strips overnight. Bound IgE antibodies were detected with alkaline phosphatase-conjugated monoclonal mouse anti-human IgE (1:750). The binding patterns were visualized with CSPD chemiluminescent (San Miguel-Moncin et al. 2003) [821]

  Protein bands were electrophoretically transferred to PVDF membranes. Membranes were blocked with 90% defatted dry milk in Tris-buffered saline (TBS) and incubated with undiluted human serum. The blots were incubated peroxidase-conjugated rabbit immunoglobulins to human e-chains. Bound peroxidase was detected by immersion in an enhanced chemiluminiscence solution (Vila et al. 1998) [823]

• Immunoblotting results:

  The Western blot revealed a protein band of 40 kDa in the extract from core but no reactivity was shown for extracts derived form leaves (Franck et al. 1999) [822]

  Sera recated with 18 different bands (13-92 kDa) (Helbling et al. 1994) [868]

  Ten of the fourteen patients (71%) showed specific IgE binding to a low molecular weight protein of 9 kDa. The IgE binding protein bands of 25 kDa and higher were detected by sera from two patients, with one also showing IgE to the 9 kDa band. One serum had a very strong reactivity to multiple lettuce proteins including the 9 kDa band. Three patients did not show IgE binding to any protein, although two of them had positive specific serum IgE to lettuce (San Miguel-Moncin et al. 2003) [821]

  Four bands of 50, 43, 39, 16 kDa could be detected (Vila et al. 1998) [823]

Oral provocation

• Number of Studies:1-5
• Food used and oral provocation vehicle:Fresh lettuce
• Blind:

  No

• Number of Patients:

  A 23-year-old woman with a history of rhinitis and swelling of her face and throat after exposure to fresh vegetables unless they were cooked. She also had strongly positive SPT to lettuce (Schwartz et al. 1995) [867]

  A 32-year-old man with a digestive and respiratory form of food allergy to lettuce and pollinosis (Franck et al. 1999) [822]

• Dose response:

  Only one dose consisting of two to three leaves of shredded Boston red lettuce (Schwartz et al. 1995) [867]

  30 g of lettuce (Franck et al. 1999) [822]

• Symptoms:

  Increase in nasal resistance (>150% of baseline) promptly after the food ingestion persisting for an hour after challenge (Schwartz et al. 1995) [867]

  Labial pruritis, dry cough and stomach pain 30 min after ingestion of lettuce. A 15% decrease in peak expiratory flow was observed 2h after (Franck et al. 1999) [822]

IgE cross-reactivity and Polysensitisation

Other Clinical information

Reviews (0)

References (6)

• Vila L, Sanchez G, Sanz ML, Dieguez I, Martinez A, Palacios R, Martinez J.
  Study of a case of hypersensitivity to lettuce (Lactuca sativa).
  Clin Exp Allergy. 28(8):1031-5.. 1998
  PUBMEDID: 9756210
• Franck P, Kanny G, Dousset B, Nabet P, Moneret-Vautrin DA.
  Lettuce allergy
  Allergy. 55(2):201-2. 2000
  PUBMEDID: 10726743
• San Miguel-Moncín M ,Krail M ,Scheurer S ,Enrique E ,Alonso R, Conti A , Cisteró-Bahíma A, Vieths S
  Lettuce anaphylaxis: identification of a lipid transfer protein as the major allergen
  Allergy 58(6): 511-517. 2003
  PUBMEDID: 12757453
• Schwartz HJ, Arnold JL, Strohl KP
  Nasal response to carrot and lettuce challenge in allergic patients
  Ann Allergy Asthma Immunol. 74(2):152-4.. 1995
  PUBMEDID: 7697474
• Helbling A, Schwartz HJ, Lopez M, Lehrer SB
  Lettuce and carrot allergy: are they related?
  Allergy Proc. 15(1):33-8.. 1994
  PUBMEDID: 8005454
• Olive-Perez A, Pineda F
  Anaphylactic reaction to 'Tudela' lettuce hearts
  Allergy. 58(11):1205-6. 2003
  PUBMEDID: 14616144

Biochemical Information for Lac s 1

• Allergen Name:Lac s 1
• Alternatve Allergen Names:
• Allergen Designation:
• Protein Family:

  Protease inhibitor/seed storage/LTP family, Pfam PF00234

  non specific lipid transfer protein (nsLTP)

• Sequence Known?:N-terminal amino acid sequence (San Miguel-Moncin et al. 2003) [821]
• Allergen accession No.s:None
• 3D Structure Accession No.:None
• Calculated Masses:Not determined
• Experimental Masses:9 kDa
• Oligomeric Masses:None
• Allergen epitopes:Not determined
• Allergen stability:
  Process, chemical, enzymatic:Most LTPs are relatively stable to heating and proteolysis (Asero et al. 2000 [10]) whilst the stability of lettuce ns-LTP has not been characterised.
• Nature of main cross-reacting proteins:Cross-reactive with rPru av 3 (Cherry LTP) and partial cross-reactivity with Platanus pollen extracts (San Miguel-Moncin et al. 2003) [821].
• 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. The helices are linked by four disulphide bridges. 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. It is possible that a lipid-like post-translational modification is involved (Lindorff-Larsen et al. 2001 [903]).
  
• Allergen purification:The allergen has not been purified.
• Other biochemical information:The N-terminal sequence of the allergen showed a high degree of amino acid sequence identity to apple LTP (Mal d 3) (ID:67% and SI:92%) (San Miguel-Moncin et al. 2003) [821].

References (3)

• San Miguel-Moncín M ,Krail M ,Scheurer S ,Enrique E ,Alonso R, Conti A , Cisteró-Bahíma A, Vieths S
  Lettuce anaphylaxis: identification of a lipid transfer protein as the major allergen
  Allergy 58(6): 511-517. 2003
  PUBMEDID: 12757453
• 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
• 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