HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Vrtala, S. Articles by Valenta, R. Search for Related Content PubMed PubMed Citation Articles by Vrtala, S. Articles by Valenta, R.

Molecular, Immunological, and Structural Characterization of Phl p 6, a Major Allergen and P-Particle-Associated Protein from Timothy Grass (Phleum pratense) Pollen¹

Susanne Vrtala^2,*, Sabine Fischer^*, Monika Grote, Luca Vangelista, Annalisa Pastore^§, Wolfgang R. Sperr^¶, Peter Valent^¶, Rudolf Reichelt, Dietrich Kraft^* and Rudolf Valenta^*

^* Institute of General and Experimental Pathology, Vienna General Hospital, University of Vienna, Vienna, Austria; Institute of Medical Physics and Biophysics, University of Münster, Münster, Germany; European Molecular Biology Laboratory, Heidelberg, Germany; ^§ Molecular Structure Division, National Institute for Medical Research, London, United Kingdom; and ^¶ Department of Internal Medicine I, Division of Hematology, Vienna General Hospital, University of Vienna, Vienna, Austria

Due to the wide distribution and heavy pollen production of grasses, 50% of allergic patients are sensitized against grass pollen allergens. cDNAs coding for two isoforms and four fragments of a major timothy grass (Phleum pratense) pollen allergen, Phl p 6, were isolated by IgE immunoscreening from a pollen expression cDNA library. Recombinant Phl p 6 (rPhl p 6), an acidic protein of 11.8 kDa, was purified to homogeneity as assessed by mass spectrometry and exhibited almost exclusive -helical secondary structure as determined by circular dichroism spectroscopy. Phl p 6 reacted with serum IgE from 75% of grass pollen-allergic patients (n = 171). IgE binding experiments with rPhl p 6 fragments indicated that the N terminus of the allergen is required for IgE recognition. Purified rPhl p 6 elicited dose-dependent basophil histamine release and immediate type skin reactions in patients allergic to grass pollen. A rabbit antiserum raised against purified rPhl p 6 identified it as a pollen-specific protein that, by immunogold electron microscopy, was localized on the polysaccharide-containing wall-precursor bodies (P-particles). The association of Phl p 6 with P-particles may facilitate its intrusion into the deeper airways and thus be responsible for the high prevalence of IgE recognition of Phl p 6. Recombinant native-like Phl p 6 can be used for in vitro as well as in vivo diagnoses of grass pollen allergy, whereas N-terminal deletion mutants with reduced IgE binding capacity may represent candidates for immunotherapy of grass pollen allergy with a low risk of anaphylactic side effects.

This article has been cited by other articles:

				S. Vrtala, M. Focke, J. Kopec, P. Verdino, A. Hartl, W. R. Sperr, A. A. Fedorov, T. Ball, S. Almo, P. Valent, et al. Genetic Engineering of the Major Timothy Grass Pollen Allergen, Phl p 6, to Reduce Allergenic Activity and Preserve Immunogenicity J. Immunol., August 1, 2007; 179(3): 1730 - 1739. [Abstract] [Full Text] [PDF]

				I. Rauter, M.-T. Krauth, S. Flicker, A. Gieras, K. Westritschnig, S. Vrtala, N. Balic, S. Spitzauer, J. Huss-Marp, K. Brockow, et al. Allergen cleavage by effector cell-derived proteases regulates allergic inflammation FASEB J, May 1, 2006; 20(7): 967 - 969. [Abstract] [Full Text] [PDF]

				T. Madan, P. Priyadarsiny, M. Vaid, N. Kamal, A. Shah, W. Haq, S. B. Katti, and P. U. Sarma Use of a Synthetic Peptide Epitope of Asp f 1, a Major Allergen or Antigen of Aspergillus fumigatus, for Improved Immunodiagnosis of Allergic Bronchopulmonary Aspergillosis Clin. Vaccine Immunol., May 1, 2004; 11(3): 552 - 558. [Abstract] [Full Text] [PDF]

				P. Karisola, J. Mikkola, N. Kalkkinen, K. J. Airenne, O. H. Laitinen, S. Repo, O. T. Pentikainen, T. Reunala, K. Turjanmaa, M. S. Johnson, et al. Construction of Hevein (Hev b 6.02) with Reduced Allergenicity for Immunotherapy of Latex Allergy by Comutation of Six Amino Acid Residues on the Conformational IgE Epitopes J. Immunol., February 15, 2004; 172(4): 2621 - 2628. [Abstract] [Full Text] [PDF]

				O. Maglio, J. W. Saldanha, S. Vrtala, S. Spitzauer, R. Valenta, and A. Pastore A major IgE epitope-containing grass pollen allergen domain from Phl p 5 folds as a four-helix bundle Protein Eng. Des. Sel., August 1, 2002; 15(8): 635 - 642. [Abstract] [Full Text] [PDF]

				S. Flicker, S. Vrtala, P. Steinberger, L. Vangelista, A. Bufe, A. Petersen, M. Ghannadan, W. R. Sperr, P. Valent, L. Norderhaug, et al. A Human Monoclonal IgE Antibody Defines a Highly Allergenic Fragment of the Major Timothy Grass Pollen Allergen, Phl p 5: Molecular, Immunological, and Structural Characterization of the Epitope-Containing Domain J. Immunol., October 1, 2000; 165(7): 3849 - 3859. [Abstract] [Full Text] [PDF]