Amino acid sequence of Fel dI, the major allergen of the domestic cat: protein sequence analysis and cDNA cloning.
Open Access
- 1 November 1991
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 88 (21) , 9690-9694
- https://doi.org/10.1073/pnas.88.21.9690
Abstract
The complete primary structure of Fel dI (International Union of Immunological Societies nomenclature), the major allergen produced by the domestic cat, Felis domesticus, was determined by protein sequence analysis and cDNA cloning. Protein sequencing of Fel dI from an immunoaffinity-purified extract of house dust revealed that the allergen is composed of two polypeptide chains. Degenerate oligonucleotides derived from the protein sequence were used in polymerase chain reaction amplification of cat salivary gland cDNA to demonstrate that the two chains are encoded by different genes. Chain 1 of Fel dI shares amino acid homology with rabbit uteroglobin, while chain 2 is a glycoprotein with N-linked oligosaccharides.Keywords
This publication has 47 references indexed in Scilit:
- The Specificity and Regulation of T-Cell Responsiveness to AllergensAnnual Review of Immunology, 1991
- Studies on the biochemical structure of the major cat allergen Felis domesticus IMolecular Immunology, 1991
- Epidemiology of acute asthma: IgE antibodies to common inhalant allergens as a risk factor for emergency room visitsJournal of Allergy and Clinical Immunology, 1989
- Immunoanalysis of histamine through a novel chemical derivatizationJournal of Allergy and Clinical Immunology, 1988
- Characterization of the Main IgE-Binding Components of Cat DanderInternational Archives of Allergy and Immunology, 1987
- Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomesCell, 1986
- A comparative study of the allergens of cat urine, serum, saliva, and peltJournal of Allergy and Clinical Immunology, 1985
- X-ray crystallographic analysis of a progesterone-binding protein. The C2221 crystal form of oxidized uteroglobin at 2.2 Å resolutionJournal of Molecular Biology, 1980
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- Pet sensitivities in asthmatic children.Archives of Disease in Childhood, 1976