Primary Structure of Lep D I, the Main Lepidoglyphus Destructor Allergen

Authors


  • Note. The novel sequence data published for Lep d I have been submitted to the EMBL data bank and are available under accession number X81399.

  • Supplementary Material. Primary structure of Lep d I, the main Lepidoglyphus destructor allergen. Fig. S1. Mass spectrometry of Lep d I. Fig. S2. Reverse-phase HPLC analysis of a tryptic digest of Lep d I. Fig. S3. Reverse-phase HPLC rechromatography of a chymotryptic digest of S -carboxymethylated Lep d I. Fig. S4. Reverse-phase HPLC analysis of a Staphylococcus aureus V8 digest of S -carboxymethylated Lep d I. Fig. S5. Reverse-phase HPLC analysis of an endoprotease Asp-N digest of S -carboxymethylated Lep d I. Fig. S6. Reverse-phase HPLC analysis of proline endopeptidase digest of peptide N-7. Fig. S7. Primers used to amplify by PCR a 3′ portion of cDNA of Lep d I. This information is available, upon request, from the Editorial Office. A total of 14 pages are available.

F. Polo, Departamento de Investigación, Alergia e Inmunología Abelló S. A., C/Miguel Fleta, 19, E-28037 Madrid, Spain

Abstract

The most relevant allergen of the storage mite Lepidoglyphus destructor (Lep d I) has been characterized. Lep d I is a monomer protein of 13273 Da. The primary structure of Lep d I was determined by N-terminal Edman degradation and partially confirmed by cDNA sequencing. Sequence polymorphism was observed at six positions, with non-conservative substitutions in three of them. No potential N-glycosylation site was revealed by peptide sequencing, The 125-residue sequence of Lep d I shows approximately 40% identity (including the six cysteines) with the overlapping regions of group II allergens from the genus Dermatophagoides, which, however, do not share common allergenic epitopes with Lep d I.

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