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

Terumi Midoro-Horiuti, R. M. Goldblum, E. G. Brooks

Research output: Contribution to journalArticle

22 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)771-778
Number of pages8
JournalClinical and Experimental Allergy
Volume31
Issue number5
DOIs
StatePublished - 2001

Fingerprint

Juniperus
Pollen
Allergens
Mutation
Genes
Oncogene Protein p65(gag-jun)
Proteins
Taxodiaceae
Immunoglobulin E
Cupressaceae
Complementary DNA
Amino Acids
Terminator Codon
Protein Sequence Analysis
Post Translational Protein Processing
Reverse Transcriptase Polymerase Chain Reaction
Glycosylation
Immunoblotting
Epitopes
Polyacrylamide Gel Electrophoresis

Keywords

  • Cedar allergy
  • Eastern red cedar
  • Jun a 1
  • Jun a 3
  • Jun v 1, Jun v 3
  • Juniperus ashei
  • Juniperus virginiana
  • Pollen allergy
  • Pollinosis

ASJC Scopus subject areas

  • Immunology

Cite this

Identification of mutations in the genes for the pollen allergens of eastern red cedar (Juniperus virginiana). / Midoro-Horiuti, Terumi; Goldblum, R. M.; Brooks, E. G.

In: Clinical and Experimental Allergy, Vol. 31, No. 5, 2001, p. 771-778.

Research output: Contribution to journalArticle

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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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N2 - 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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