cDNA Cloning and Sequencing Reveal the Major Horse Allergen Equ c1 to Be a Glycoprotein Member of the Lipocalin Superfamily
| Autor: | Christophe Grégoire, Bernard David, J. Rabillon, J.-P. Dandeu, Pedro M. Alzari, Isabelle Rosinski-Chupin |
|---|---|
| Přispěvatelé: | Immuno-Allergie, Institut Pasteur [Paris], lmmunologie structurale, Institut Pasteur [Paris] (IP) |
| Jazyk: | angličtina |
| Rok vydání: | 1996 |
| Předmět: |
Models
Molecular MESH: Sequence Homology Amino Acid MESH: Amino Acid Sequence Lipocalin MESH: Base Sequence Biochemistry law.invention MESH: Recombinant Proteins 0302 clinical medicine law Tissue Distribution MESH: Animals Cloning Molecular Peptide sequence chemistry.chemical_classification 0303 health sciences [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM] MESH: Salivary Proteins and Peptides MESH: Lipoproteins Lipocalins Recombinant Proteins 3. Good health Multigene Family Recombinant DNA MESH: Lipocalins Antibody MESH: Models Molecular DNA Complementary MESH: Allergens medicine.drug_class Lipoproteins [PHYS.PHYS.PHYS-BIO-PH]Physics [physics]/Physics [physics]/Biological Physics [physics.bio-ph] Molecular Sequence Data MESH: Glycoproteins [SDV.BC]Life Sciences [q-bio]/Cellular Biology Biology Monoclonal antibody 03 medical and health sciences Complementary DNA medicine [CHIM.CRIS]Chemical Sciences/Cristallography Animals Humans MESH: Cloning Molecular [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Amino Acid Sequence Horses Salivary Proteins and Peptides MESH: Tissue Distribution MESH: Horses Molecular Biology Glycoproteins 030304 developmental biology MESH: Humans MESH: Molecular Sequence Data Base Sequence Sequence Homology Amino Acid Cell Biology MESH: DNA Complementary Allergens Molecular biology MESH: Solubility Solubility 030228 respiratory system chemistry Polyclonal antibodies biology.protein MESH: Multigene Family [INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM] Glycoprotein |
| Zdroj: | Journal of Biological Chemistry Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 1996, 271 (51), pp.32951-32959. ⟨10.1074/jbc.271.51.32951⟩ Journal of Biological Chemistry, 1996, 271 (51), pp.32951-32959. ⟨10.1074/jbc.271.51.32951⟩ |
| ISSN: | 0021-9258 1083-351X |
| DOI: | 10.1074/jbc.271.51.32951⟩ |
| Popis: | International audience; The gene encoding the major horse allergen, designated Equus caballus allergen 1 (Equ c1), was cloned from total cDNA of sublingual salivary glands by reverse transcription-polymerase chain reaction using synthetic degenerate oligonucleotides deduced from N-terminal and internal peptide sequences of the glycosylated hair dandruff protein. A recombinant form of the protein, with a polyhistidine tail, was expressed in Escherichia coli and purified by immobilized metal affinity chromatography. The recombinant protein is able to induce a passive cutaneous anaphylaxis reaction in rat, and it behaves similarly to the native Equ c1 in several immunological tests with allergic patients' IgE antibodies, mouse monoclonal antibodies, or rabbit polyclonal IgG antibodies. Amino acid sequence identity of 49-51% with rodent urinary proteins from mice and rats suggests that Equ c1 is a new member of the lipocalin superfamily of hydrophobic ligand-binding proteins that includes several other major allergens. An RNA blot analysis demonstrates the expression of mRNA Equ c1 in liver and in sublingual and submaxillary salivary glands. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|