Characterization of the allergen group VI in timothy grass pollen (Phl p 6). I. Immunological and biochemical studies.
For the identification and characterization of allergen grass group VI we performed two-dimensional immunoblotting of timothy grass pollen (Phleum pratense). Two intense 13-kD protein spots of pI 5.2 and 5.5 were found to be IgE reactive. By N-terminal microsequencing and amino acid analysis we identified them as Phl p 6 isoallergens. An antiserum was raised against Phl p 6 by immunizing BALB/c mice with allergen bearing nitrocellulose particles of one isoform. The antiserum revealed an intense reactivity to Phl p 6 isoforms, but also showed a weak cross-reactivity with Phl p 5 allergens. After immunoabsorption of patients' serum to Phl p 6 spots on the blotting membrane, we were able to demonstrate that the eluted human IgE antibodies cross-react with the grass group V allergens as well. Therefore, Phl p 5 and Phl p 6 possess one or more common IgE binding epitopes.
Petersen
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Division of Allergology, Forschungsinstitut Borstel, Germany.
Bufe
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Schlaak
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Becker
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WM
D000485:Allergens; D000595:Amino Acid Sequence; D000818:Animals; D000939:Epitopes / Q000737:chemistry; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics* / Q000276:immunology; D006109:Poaceae / Q000737:chemistry* / Q000276:immunology*; D011058:Pollen / Q000737:chemistry* / Q000276:immunology*; D011817:Rabbits
D000485:Allergens; D000939:Epitopes; C095238:PHLPVI protein, Phleum pratense; C076049:Phl p V protein, Phleum pratense; D010940:Plant Proteins