Blessy Maruthukunnel Mani1, Jose Angel Huerta-Ocampo2, Jose Ruben Garcia-Sanchez1, Alberto Barrera-Pacheco3, Ana Paulina Barba de la Rosa3, Luis M Teran4. 1. Escuela Superior de Medicina del Instituto Politécnico Nacional, Plan de San Luis y Díaz Mirón, Casco de Santo Tomás, C.P.11340 México City, Mexico. 2. Centro de investigación en Alimentación y Desarrollo, A.C. Apartado Postal 1735, Hermosillo, Sonora, Mexico. 3. División Biología Molecular, IPICyT, Instituto Potosino de Investigación Científica y Tecnológica, Camino a la Presa San José 2055, Col. Lomas 4a. Sección, 78216 San Luis Potosí, SLP, Mexico. 4. Instituto Nacional de Enfermedades Respiratorias "Ismael Cosío Villegas", Calzada Tlalpan No. 4502, Sección XVI, C.P.14080 México City, Mexico. Electronic address: teranjlm@gmail.com.
Abstract
BACKGROUND: Ligustrum spp. are members of the Oleaceae family, one of the most prominent allergic families worldwide. The genus Ligustrum contains approximately fifty species, including Ligustrum lucidum, which have been widely cultivated as ornamental plants, and its pollen is a source of inhalant allergens associated with respiratory allergic diseases. Little is known about the presence of allergenic proteins in L. lucidum. METHODS: The L. lucidum pollen proteins were extracted by a modified phenolic extraction method. A pool of four sera from mono sensitive patients was analyzed by 2DE immunoblotting and mass spectrometric analysis was performed on 6 immunoreactive protein spots. RESULTS: SDS-PAGE of L. lucidum pollen extract revealed proteins in ranges of 15-150 kDa. The 2DE gel profile of the L. lucidum pollen protein extract showed approximately 180 spots, and the 2DE immunoblots obtained using sera from Ligustrum monosensitive patients as the source of IgE antibodies revealed six allergen protein spots, corresponding to Profilin, Enolase, Fra e 9.01 (β-1,3-glucanase), Pollen-specific Polygalacturonases, Alanine aminotransferase, and two ATP synthase beta subunits. CONCLUSION: We report for the first time the identification of IgE-reactive proteins from L. lucidum.
BACKGROUND:Ligustrum spp. are members of the Oleaceae family, one of the most prominent allergic families worldwide. The genus Ligustrum contains approximately fifty species, including Ligustrum lucidum, which have been widely cultivated as ornamental plants, and its pollen is a source of inhalant allergens associated with respiratory allergic diseases. Little is known about the presence of allergenic proteins in L. lucidum. METHODS: The L. lucidum pollen proteins were extracted by a modified phenolic extraction method. A pool of four sera from mono sensitive patients was analyzed by 2DE immunoblotting and mass spectrometric analysis was performed on 6 immunoreactive protein spots. RESULTS:SDS-PAGE of L. lucidum pollen extract revealed proteins in ranges of 15-150 kDa. The 2DE gel profile of the L. lucidum pollen protein extract showed approximately 180 spots, and the 2DE immunoblots obtained using sera from Ligustrum monosensitive patients as the source of IgE antibodies revealed six allergen protein spots, corresponding to Profilin, Enolase, Fra e 9.01 (β-1,3-glucanase), Pollen-specific Polygalacturonases, Alanine aminotransferase, and two ATP synthase beta subunits. CONCLUSION: We report for the first time the identification of IgE-reactive proteins from L. lucidum.
Authors: José Ángel Huerta-Ocampo; Alejandra Valenzuela-Corral; María Del Refugio Robles-Burgueño; Ana María Guzmán-Partida; Miguel Ángel Hernández-Oñate; Luz Vázquez-Moreno; Gandhi F Pavón-Romero; Luis M Terán Journal: World Allergy Organ J Date: 2020-03-17 Impact factor: 4.084
Authors: Gandhi F Pavón-Romero; Maria Itzel Parra-Vargas; Fernando Ramírez-Jiménez; Esmeralda Melgoza-Ruiz; Nancy H Serrano-Pérez; Luis M Teran Journal: Cells Date: 2022-01-08 Impact factor: 6.600