The dominant 55kDa allergen of the subtropical Bahia grass (Paspalum notatum) pollen is a group 13 pollen allergen, Pas n 13

Davies, Janet M., Voskamp, Astrid, Dang, Thanh D., Pettit, Benjamin, Loo, Dorothy, Petersen, Arnd, Hill, Michelle M., Upham, John W., Rolland, Jennifier M., & O'Hehir, Robyn E. (2011) The dominant 55kDa allergen of the subtropical Bahia grass (Paspalum notatum) pollen is a group 13 pollen allergen, Pas n 13. Molecular Immunology, 48(6-7), pp. 931-940.

View at publisher


Bahia grass, Paspalum notatum, is an important pollen allergen source with a long season of pollination and wide distribution in subtropical and temperate regions. We aimed to characterize the 55. kDa allergen of Bahia grass pollen (BaGP) and ascertain its clinical importance. BaGP extract was separated by 2D-PAGE and immunoblotted with serum IgE of a grass pollen-allergic patient. The amino-terminal protein sequence of the predominant allergen isoform at 55. kDa had similarity with the group 13 allergens of Timothy grass and maize pollen, Phl p 13 and Zea m 13. Four sequences obtained by rapid amplification of the allergen cDNA ends represented multiple isoforms of Pas n 13. The predicted full length cDNA for Pas n 13 encoded a 423 amino acid glycoprotein including a signal peptide of 28 residues and with a predicted pI of 7.0. Tandem mass spectrometry of tryptic peptides of 2D gel spots identified peptides specific to the deduced amino acid sequence for each of the four Pas n 13 cDNA, representing 47% of the predicted mature protein sequence of Pas n 13. There was 80.6% and 72.6% amino acid identity with Zea m 13 and Phl p 13, respectively. Reactivity with a Phl p 13-specific monoclonal antibody AF6 supported designation of this allergen as Pas n 13. The allergen was purified from BaGP extract by ammonium sulphate precipitation, hydrophobic interaction and size exclusion chromatography. Purified Pas n 13 reacted with serum IgE of 34 of 71 (48%) grass pollen-allergic patients and specifically inhibited IgE reactivity with the 55. kDa band of BaGP for two grass pollen-allergic donors. Four isoforms of Pas n 13 from pI 6.3-7.8 had IgE-reactivity with grass pollen allergic sera. The allergenic activity of purified Pas n 13 was demonstrated by activation of basophils from whole blood of three grass pollen-allergic donors tested but not control donors. Pas n 13 is thus a clinically relevant pollen allergen of the subtropical Bahia grass likely to be important in eliciting seasonal allergic rhinitis and asthma in grass pollen-allergic patients.

Impact and interest:

5 citations in Scopus
Search Google Scholar™
6 citations in Web of Science®

Citation counts are sourced monthly from Scopus and Web of Science® citation databases.

These databases contain citations from different subsets of available publications and different time periods and thus the citation count from each is usually different. Some works are not in either database and no count is displayed. Scopus includes citations from articles published in 1996 onwards, and Web of Science® generally from 1980 onwards.

Citations counts from the Google Scholar™ indexing service can be viewed at the linked Google Scholar™ search.

ID Code: 87909
Item Type: Journal Article
Refereed: Yes
Keywords: Bahia grass pollen, Grass pollen allergens, Group 13 pollen allergen, IgE, Pas n 13, Polygalacturonase, ammonium sulfate, complementary DNA, grass pollen antigen, immunoglobulin E, pollen antigen, unclassified drug, allergen, peptide, vegetable protein, amino acid sequence, amino terminal sequence, antigen purification, article, basophil, cell activation, controlled study, gene amplification, grass pollen, human, human cell, hydrophobicity, major clinical study, nucleotide sequence, Paspalum, Paspalum notatum, pollen allergy, priority journal, sequence alignment, sequence analysis, blood, chemistry, DNA sequence, donor, genetics, immunology, isolation and purification, mass spectrometry, molecular genetics, molecular weight, pollen, polymerase chain reaction, tropic climate, two dimensional gel electrophoresis, Phleum pratense, Zea, Zea mays, Allergens, Basophils, DNA, Complementary, Electrophoresis, Gel, Two-Dimensional, Humans, Molecular Sequence Data, Peptides, Plant Proteins, Sequence Analysis, DNA, Tissue Donors, Tropical Climate
DOI: 10.1016/j.molimm.2010.12.013
ISSN: 0161-5890
Divisions: Current > Schools > School of Biomedical Sciences
Current > QUT Faculties and Divisions > Faculty of Health
Current > Institutes > Institute of Health and Biomedical Innovation
Deposited On: 30 Sep 2015 05:01
Last Modified: 01 Oct 2015 04:41

Export: EndNote | Dublin Core | BibTeX

Repository Staff Only: item control page