Olive (Olea europea) and privet (Ligustrum vulgare) pollen allergens. Identification and cross-reactivity with grass pollen proteins

Mol Immunol. 1992 Oct;29(10):1209-18. doi: 10.1016/0161-5890(92)90057-5.

Abstract

Protein blotting studies showed that three olive pollen components with mol. wts approximately 18-19, 20 and 40 kD can be considered to be major allergens. For privet pollen, the highest recognition frequencies were for allergens of mol. wts approximately 20, approximately 19, approximately 40 and approximately 70 kD. When results with the 62 subjects examined were separated into groups corresponding to their geographical locations, viz. Italy, France and Australia, subjects sensitized to olive, but not other pollens (some Italian subjects), were found to show higher frequencies of recognition of major olive allergens than subjects sensitized to olive pollen via cross-reacting allergens from unrelated pollen sources (the Australian and French subjects). Blotting, adsorption and elution and inhibition studies clearly demonstrated allergenic cross-reactivity (that is, antigenic cross-reactivity detected by IgE antibodies) between olive, privet, ryegrass (Lolium perenne) and couch grass (Bermuda grass: Cynodon dactylon) pollen components. As with our previous findings with birch pollen, we conclude that the presence of pollen-reactive IgE antibodies may not necessarily be a true reflection of the sensitizing pollen species.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allergens / immunology*
  • Australia
  • Blotting, Western
  • Cross Reactions
  • France
  • Humans
  • Immunoglobulin E / blood
  • Immunoglobulin E / immunology
  • Immunologic Memory
  • Italy
  • Molecular Weight
  • Poaceae
  • Pollen / immunology*
  • Radioallergosorbent Test
  • Rhinitis, Allergic, Seasonal / immunology*
  • Trees

Substances

  • Allergens
  • Immunoglobulin E