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標題: A pollen-specific polygalacturonase from lily is related to major grass pollen allergens
作者: Chiang, J.Y.
Balic, N.
Hsu, S.W.
Yang, C.Y.
Ko, C.W.
Hsu, Y.F.
Swoboda, I.
Wang, C.S.
關鍵字: allergen;gene expression;IgE cross-reactivity;Lilium longiflorum;pollen-specific;polygalacturonase;lilium-longiflorum pollen;messenger-rnas;tube growth;molecular;characterization;pectin methylesterase;male gametophyte;gene-expression;phleum-pratense;p 13;protein
Project: Plant Physiology and Biochemistry
期刊/報告no:: Plant Physiology and Biochemistry, Volume 44, Issue 11-12, Page(s) 743-751.
A pollen-specific gene from lily (Lilium longiflorum Thunb. cv. Snow Queen), designated LLP-PG, was characterized. Southern blots of lily genomic DNA indicated that LLP-PG is a member of a small gene family. A thorough sequence analysis revealed that the LLP-PG gene is interrupted by two introns and encodes a protein of 413 amino acids, with a calculated molecular mass of 44 kDa, and a pI of 8.1. Evaluation of the hydropathy profile showed that the protein has a hydrophobic segment at the N-terminus, indicating the presence of a putative signal peptide. A sequence similarity search showed a significant homology of the encoded protein to pollen polygalacturonases (PGs) from various plant species and to an important group (group 13) of grass pollen allergens. The LLP-PG transcript is pollen-specific and it accumulates only at the latest stage during pollen development, in the mature pollen. In contrast to other "late genes" LLP-PG transcript can neither be induced by abscisic acid (ABA) nor by dehydration. Immunoblot analyses of pollen protein extracts from lily, timothy grass and tobacco with IgG antibodies directed against LLP-PG and against the timothy grass pollen allergen, Phl p 13, indicated that lily LLP-PG shares surface-exposed epitopes with pollen PGs from monocotyledonous and dicotyledonous plants. Enzyme-linked immunosorbent assay (ELISA) analyses and inhibition ELISA assays with patients' IgE demonstrated a very low IgE reactivity of lily rLLP-PG and a lack of cross-reactivity between rLLP-PG and the timothy grass pollen allergen, rPhl p 13. These data demonstrated that despite the significant sequence homology and the conserved surface-exposed epitopes LLP-PG represents a low-allergenic member of pollen PGs. (c) 2006 Elsevier Masson SAS. All rights reserved.
ISSN: 0981-9428
DOI: 10.1016/j.plaphy.2006.10.005
Appears in Collections:生物科技學研究所

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