role of allergenic proteins Pla a 1 and Pla a 2 in the germination of Platanus acerifolia pollen grains

• Published in: Sexual plant reproduction 2005-11, Vol.18 (3), p.101-112
• Main Authors: Suarez-Cervera, M, Asturias, J.A, Vega-Maray, A, Castells, T, Lopez-Iglesias, C, Ibarrola, I, Arilla, M.C, Gabarayeva, N, Seoane-Camba, J.A
• Format: Article
• Language: English
• Subjects: allergens; beta-fructofuranosidase; chemical constituents of plants; developmental stages; enzyme inhibitors; fertilization (reproduction); immunocytochemistry; pectinesterase; plant anatomy; plant proteins; plant reproduction; Platanus acerifolia; poisonous plants; pollen; pollen germination; pollination; sexual reproduction; ultrastructure
• ISSN: 0934-0882; 1432-2145
• DOI: 10.1007/s00497-005-0002-4

Platanus acerifolia (Aiton) Willdenow is a plane tree, widely grown as an ornamental tree in many cities of the United States and Western Europe, which has become an important source of airborne allergens in our cities. The aim of the present study is to immunolocalize the major allergens in the pollen grain and to examine their potential function in the fertilization process. Observations were made in mature and hydrated, activated pollen of P. acerifolia for 5, 15, 30 min and 2 h in the germination medium. Specimens were fixed using freezing protocols for transmission electron microscopy (TEM). For immunogold labelling, cryosections and resin-embedded ultrathin sections were incubated using rabbit antisera against the purified pollen allergens Pla a 1 and Pla a 2. Elution of P. acerifolia allergens took place after 5 min of pollen incubation in buffered medium. Intense labelling of Pla a 1 and Pla a 2 was detected after pollen exudates were released. In pollen grains, Pla a 1 was predominantly localized in concentric cisternae of the endoplasmic reticulum (ER), situated between the vegetative nucleus and the generative cell, and was released from pollen grains 5 min after hydration; cytoplasmic localization decreased 15 min after hydration. In pollen grains, glycoprotein Pla a 2 was abundant in association with Golgi cisternae and vesicles situated in the apertural periphery of the mature pollen grains. Pla a 2 proteins were also detected in ER and in the generative cell wall. Immunolabelling of Pla a 2 decreased 5 min after pollen hydration but was again intense after 15-30 min in germination medium, presumably as a consequence of renewed expression and glycosylation of this protein. Pla a 1 belongs to a new class of allergens related to proteinaceous invertase and pectin methyl esterase inhibitors (PII, PMEI) which could be involved in membrane protection and pectin de-esterification control during pollen hydration. Pla a 2 has an exopolygalacturonase (PG) enzymatic activity consistent with pollen-stigma adhesion mechanisms or compatibility systems. Moreover, the expression of Pla a 2 found 15-30 min after hydration might contribute to pollen-tube growth and the modification of transmitting tissue cell walls. The abundant production and elution of Pla a 1 and Pla a 2 proteins may alter the environment in which pollen tube elongation occurs, thus promoting a potential crosstalk between the pollen and the gynoecium.