Literature DB >> 11422137

Identification of mutations in the genes for the pollen allergens of eastern red cedar (Juniperus virginiana).

T Midoro-Horiuti1, R M Goldblum, E G Brooks.   

Abstract

BACKGROUND: Cedar pollens are important causes of seasonal allergic disease in diverse geographical areas. However, pollens from different families and species vary in their propensity to induce allergic responses.
OBJECTIVE: To compare the structure of potential allergens from eastern red cedar (Juniperus virginiana) pollen with those of the highly allergenic cedar (mountain cedar, J. ashei) pollens.
MATERIALS AND METHODS: The cDNAs for potential pollen allergens, Jun v 1 and Jun v 3, were amplified by reverse transcriptase-polymerase chain reaction, cloned and sequenced. Expression of the native proteins in pollen was characterized by SDS-PAGE and immunoblotting.
RESULTS: The cDNA sequence for one potential major allergen, Jun v 1, was highly homologous to those of the other cedar pollens. The second potential allergen, Jun v 3, was also highly homologous to its counterpart in mountain cedar, but a stop codon in the mRNA would result in a protein of only 91 amino acids, which would lack potential N-glycosylation sites and the IgE binding epitopes of the 199 amino acid homologue from mountain cedar pollen, Jun a 3. IgE from the sera of patients with hypersensitivity to cedar pollen bound to eastern red cedar proteins of four different sizes. N-terminal amino acid sequence analysis indicated that two of these proteins (43 and 30 kDa) were either isoforms or processed Jun v 1. No Jun v 3 protein was detected. The N-terminal sequence of an additional 145-kDa allergen, termed Jun v 4, was not homologous to any previously described allergens.
CONCLUSION: These findings suggest that mutations in the genes or post-translational modifications of two potentially allergenic proteins might help to explain why the pollen of eastern red cedar is reported to be less allergenic than those of other members of Cupressaceae and Taxodiaceae families.

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Year:  2001        PMID: 11422137     DOI: 10.1046/j.1365-2222.2001.01079.x

Source DB:  PubMed          Journal:  Clin Exp Allergy        ISSN: 0954-7894            Impact factor:   5.018


  5 in total

1.  Crystal structure of Jun a 1, the major cedar pollen allergen from Juniperus ashei, reveals a parallel beta-helical core.

Authors:  Edmund W Czerwinski; Terumi Midoro-Horiuti; Mark A White; Edward G Brooks; Randall M Goldblum
Journal:  J Biol Chem       Date:  2004-11-10       Impact factor: 5.157

2.  Structural basis for epitope sharing between group 1 allergens of cedar pollen.

Authors:  Terumi Midoro-Horiuti; Catherine H Schein; Venkatarajan Mathura; Werner Braun; Edmund W Czerwinski; Akihisa Togawa; Yasuto Kondo; Tetsuo Oka; Masanao Watanabe; Randall M Goldblum
Journal:  Mol Immunol       Date:  2005-06-21       Impact factor: 4.407

3.  Isolation and characterization of native Cry j 3 from Japanese cedar (Cryptomeria japonica) pollen.

Authors:  T Fujimura; N Futamura; T Midoro-Horiuti; A Togawa; R M Goldblum; H Yasueda; A Saito; K Shinohara; K Masuda; K Kurata; M Sakaguchi
Journal:  Allergy       Date:  2007-05       Impact factor: 13.146

Review 4.  Current overview of allergens of plant pathogenesis related protein families.

Authors:  Mau Sinha; Rashmi Prabha Singh; Gajraj Singh Kushwaha; Naseer Iqbal; Avinash Singh; Sanket Kaushik; Punit Kaur; Sujata Sharma; Tej P Singh
Journal:  ScientificWorldJournal       Date:  2014-02-16

Review 5.  Tree pollen allergens-an update from a molecular perspective.

Authors:  C Asam; H Hofer; M Wolf; L Aglas; M Wallner
Journal:  Allergy       Date:  2015-08-06       Impact factor: 13.146

  5 in total

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