title: Immunochemical characterization of Russian thistle (Salsola kali) pollen extracts. Purification of the allergen Sal k 1.
abstract: BACKGROUND
  Salsola kali (Russian thistle) is a weed which belongs to the Chaenopodiacea family. It is widely distributed along the coasts of Europe, North Africa, USA and Australia. The objectives of this study were to study the allergenic composition of S. kali pollen and to purify an important allergen from the pollen extracts of this plant.
  
  
  METHODS
  A population of 66 individuals with specific IgE-mediated allergic symptoms and positive skin tests to S. kali were included in the study. Specific IgE to S. kali was determined by direct enzyme-linked immunosorbent assay (ELISA). The antigenic and allergenic profile of S. kali was evaluated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), isoelectric focussing (IEF) and immunoblot. Allergen purification was conducted by preparative SDS-PAGE. The allergenicity of the protein was evaluated by skin testing, direct ELISA, ELISA inhibition and immunoblots.
  
  
  RESULTS
  Specific IgE to S. kali was detected in 39 of the 66 individuals (59%). An allergen with a molecular weight of approximately 43 kDa was purified. This allergen was termed Sal k 1. A partial sequencing was obtained and no homology was found with other known proteins/allergens. The allergenicity of Sal k 1 was tested in vitro and in vivo. Of the 39 individuals with a positive specific IgE determination to S. kali, 26 (66.6%) had detectable specific IgE to Sal k 1. Twenty of these 39 individuals were skin-prick tested with the purified allergen (0.5 mg/ml) and all of them had a positive skin test to the purified allergen. Ten additional individuals, used as negative controls, had a negative response.
  
  
  CONCLUSIONS
  Sal k 1, an important allergen of S. kali, is recognized, in vitro, by approximately 67% of the patients sensitized to S. kali. Twenty patients with a positive skin test to a standardized S. kali extract had a positive reaction to the purified allergen.
authors: C.B.F. LETI, S.A. Research Laboratories, Tres Cantos, Madrid, Spain.
authors: J
authors: J
authors: Carnés
authors: E
authors: E
authors: Fernández-Caldas
authors: A
authors: A
authors: Marina
authors: C
authors: C
authors: Alonso
authors: C
authors: C
authors: Lahoz
authors: C
authors: C
authors: Colás
authors: A
authors: A
authors: Lezaun
mesh_terms: D000485:Allergens / Q000737:chemistry / Q000276:immunology* / Q000302:isolation & purification; D000595:Amino Acid Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D006801:Humans; D015151:Immunoblotting; D007073:Immunoglobulin E / Q000097:blood; D007525:Isoelectric Focusing; D011058:Pollen / Q000737:chemistry / Q000276:immunology*; D012130:Respiratory Hypersensitivity / Q000276:immunology; D031248:Salsola / Q000737:chemistry / Q000276:immunology*; D012882:Skin Tests
chemical_list: D000485:Allergens; D007073:Immunoglobulin E