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Complementary DNA cloning of the predominant allergen of bovine dander: A new member in the lipocalin family  Rauno Mäntyjärvi, MD, Sinikka Parkkinen,

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Presentation on theme: "Complementary DNA cloning of the predominant allergen of bovine dander: A new member in the lipocalin family  Rauno Mäntyjärvi, MD, Sinikka Parkkinen,"— Presentation transcript:

1 Complementary DNA cloning of the predominant allergen of bovine dander: A new member in the lipocalin family  Rauno Mäntyjärvi, MD, Sinikka Parkkinen, PhD, Marja Rytkönen, MSc, Jaana Pentikäinen, PhD, Jukka Pelkonen, MD, Jaakko Rautiainen, MSc, Thomas Zeiler, MD, Tuomas Virtanen, MD  Journal of Allergy and Clinical Immunology  Volume 97, Issue 6, Pages (June 1996) DOI: /S (96) Copyright © 1996 Mosby, Inc. Terms and Conditions

2 FIG. 1 Nucleotide and amino acid sequence of the longest open reading frame in the cDNA clone Pot12. Numbers above the sequence indicate nucleotides. The first methionine of this open reading frame is at codon 19. The stop codon is marked with a dot. Amino acid sequences obtained from peptide sequencing of the native BDA20 protein are underlined. Journal of Allergy and Clinical Immunology  , DOI: ( /S (96) ) Copyright © 1996 Mosby, Inc. Terms and Conditions

3 FIG. 2 Immunoblotting of the recombinant BDA20 protein expressed in E. coli. The slots contained glutathione transferase (GTS) expressed in E. coli, crude extract of bovine dander (BEA), or recombinant GST-BDA20 fusion protein (GST-BDA20). mAb refers to a monoclonal antibody prepared against native BDA20, and human IgE refers to IgE immunoblotting with the serum from a patient highly allergic to cattle. Journal of Allergy and Clinical Immunology  , DOI: ( /S (96) ) Copyright © 1996 Mosby, Inc. Terms and Conditions

4 FIG. 3 Amino acid homology comparison of the BDA20 protein as deduced from the cDNA sequence and four lipocalins. Proteins were aligned, and consensus sequence was determined by using the CGC Sequence Analysis Software Package.23 Amino acids 29 to 31 of BDA20 (GEW) represent the core of one of the highly conserved sequences of lipocalins. Lipocalins shown are rat probasin precursor (pbas_rat), rat odorant binding protein precursor (obp_rat), bovine odorant-binding protein (obp_bovin) and hamster aphrodisin (aphr_crisp). Journal of Allergy and Clinical Immunology  , DOI: ( /S (96) ) Copyright © 1996 Mosby, Inc. Terms and Conditions

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