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Isolation and characterization of an olive allergen-like protein from lilac pollen

Sequence analysis of three cDNA encoding protein isoforms

  1. Eva BATANERO1,
  2. Mayte VILLALBA1,
  3. Carlos LÓPEZ-OTÍN2,
  4. Rosalía RODRÍGUEZ1,*

Article first published online: 3 MAR 2005

DOI: 10.1111/j.1432-1033.1994.tb18728.x

Issue

European Journal of Biochemistry

European Journal of Biochemistry

Volume 221, Issue 1, pages 187–193, April 1994

Additional Information

How to Cite

BATANERO, E., VILLALBA, M., LÓPEZ-OTÍN, C. and RODRÍGUEZ, R. (1994), Isolation and characterization of an olive allergen-like protein from lilac pollen. European Journal of Biochemistry, 221: 187–193. doi: 10.1111/j.1432-1033.1994.tb18728.x

Author Information

  1. 1

    Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias, Universidad Complutense, Madrid, Spain

  2. 2

    Departamento de Biología Functional, Facultad de Medicina, Universidad de Oviedo, Oviedo, Spain

*Correspondence to R. Rodríguez, Departamento de Bioquímica y Biología Molecular, Facultad de Química, Universidad Complutense, E-28040 Madrid, Spain. Fax: +31 1 3944159.

  1. Note. The novel nucleotide sequence data published here have been submitted to the EMBL sequence data bank(s) and are available under accession number(s) X76539, X76540, X76541.

Publication History

  1. Issue published online: 3 MAR 2005
  2. Article first published online: 3 MAR 2005
  3. (Received December 7, 1993/January 24, 1994) – EJB 93 1816/3

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Abstract

  1. Top of page
  2. Abstract
  3. REFERENCES

An olive allergen-like protein has been isolated from lilac (Syringa vulgaris) pollen extract. The protein can be considered as an allergen since is recognized by IgE from olive hypersensitive human sera, and has been called Syr v I (IUIS nomenclature). This protein consists of a glycosylated polypeptide of 20 kDa, which has an amino acid composition, spectroscopic properties, and an N-terminal sequence similar to the major allergen from olive pollen, Ole e I. The lilac allergen is recognized by rabbit polyclonal antisera raised against olive allergen as well as by an Ole e I-specific monoclonal antibody. Using a polymerase chain reaction strategy, based on the similarities observed between these olive and lilac proteins, three cDNA clones encoding Syr v I have been isolated and sequenced. These clones code for a polymorphic protein of 145 residues with a derived molecular mass of about 16400Da, which contains a potential N-glycosylation site. Comparison of the deduced amino acid sequences of these Syr v I isoforms to each other revealed identities of 90–97%. Moreover, these sequences showed a high degree of similarity (85.5–89.6% identity) with Ole e I. The structural and immunological characterization of Syr v I justify the cross-reactions observed between olive and lilac pollen extracts. The molecular cloning of Syr v I is relevant for the epitope mapping in Oleacease allergens, and may contribute to an improvement in the design of reagents for diagnosis and therapy of IgE-dependent allergic reactions.

Abbreviations
HRPO

horseradish peroxidase

PCR

polymerase chain reaction

Enzymes
 

Restriction endonucleases EcoRI and BamHI (EC 3.1.21.4)

 

reverse transcriptase (EC 2.7.7.49)

 

Taq polymerase, DNA polymerase from Thermophilus aquaticus (EC 2.7.7.7)

REFERENCES

  1. Top of page
  2. Abstract
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