Immunochemical Characterization of Ligustrum Vulgare (Privet) Pollen Allergens: Study of Common Allergenic Plant in Iran

Haleh  Abdoli Sereshki; Reza Falak; Mohammad-Ali Assarehzadegan; Mohammad Nabavi; Mohammad-Hossein Shams; Maral Ranjbar

doi:10.18502/ijaai.v21i1.8615

Haleh Abdoli Sereshki Immunology Research Center, Institute of Immunology and Infectious Diseases, Iran University of Medical Sciences, Tehran, Iran
Reza Falak Immunology Research Center, Institute of Immunology and Infectious Diseases, Iran University of Medical Sciences, Tehran, Iran
Mohammad-Ali Assarehzadegan Immunology Research Center, Institute of Immunology and Infectious Diseases, Iran University of Medical Sciences, Tehran, Iran
Mohammad Nabavi Department of Allergy and Clinical Immunology, Rasool-E-Akram Hospital, Iran University of Medical Sciences, Tehran, Iran
Mohammad-Hossein Shams Department of Medical Immunology, School of Medicine, Lorestan University of Medical Sciences, Khorramabad, Iran
Maral Ranjbar Department of Medicine, Mc Master University, Hamilton, Canada

DOI: https://doi.org/10.18502/ijaai.v21i1.8615

Keywords: Allergens; Iran; Ligustrum; Prevalence; Pollen

Abstract

Ligustrum vulgare (Privet) pollen proteins are responsible for allergies in susceptible individuals in many regions of the world. This study investigated the immunochemical characterization of Privet pollen extract and the occurrence of skin prick test reactivity to Privet and other allergenic pollen grains in allergic rhinitis patients.

All subjects experienced a skin prick test with twenty-two allergen extracts. sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) separated Privet pollen extract, IgE-immunoblotting, and specific ELISA procedures determined the allergenic profile on forty-five Privet allergic patients.

A positive allergic reaction to L. vulgare pollen extract was observed in forty-five (31.4%) out of 145 patients. Ten resolved protein fractions were found on SDS-PAGE, ranging from 10 to 80 kDa. IgE-specific antibodies interacted with several allergenic protein bands from Privet-allergic patients in the immunoblotting assay. The most significant interaction was observed in proteins with molecular weights of approximately 15, 18, 43, and 66 kDa.

Privet pollen is regarded as a potent allergen composed of IgE-binding constituents. Considering the high allergenicity of Privet pollen grains and since many countries are rich in this plant, identification and production of recombinant forms of common allergens in this species can be used for developing more efficient diagnostic, therapeutic, and preventive approaches.