Vegetable Proteomics: The Detection of Ole e 1 Isoallergens by Peptide Matching of MALDI MS/MS Spectra of Underivatized and Dansylated Glycopeptides

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• 作者：Anna Napoli ; Donatella Aiello ; Leonardo Di Donna ; Petros Moschidis ; Giovanni Sindona
• 刊名：Journal of Proteome Research
• 出版年：2008
• 出版时间：July 2008
• 年：2008
• 卷：7
• 期：7
• 页码：2723 - 2732
• 全文大小：1184K
• 年卷期：v.7,no.7(July 2008)
• ISSN：1535-3907

文摘

Ole e 1 (NCBI entry gi|14424429) is the major allergen of Oleaceae family. Multiple isoforms and variants are present in varying degrees of distribution. In this report, we present a new approach to the resolution of multiple forms of Ole e 1 from whole antigen extracts, based on a preliminary chemical fractionation procedure followed by MALDI MS and MS/MS measurements. The characterization of Ole e 1 isoallergens was accomplished through the identification of the amino acid sequence including the glycosylation site and the structure of the glycan moieties. The structure feature of the identified Ole e 1.0102 (gi|2465127), main olive allergen [Olea europaea] (gi|13195753), Major pollen allergen Ole e 1 (gi|33329740) and Ole e 1c (gi|1362131) is represented by the point mutation K₁₀₆ → I and by the presence of a glycan moiety. Two other variants Major pollen allergen (Allergen Ole e1) (Ole e I) (gi|14424429) and Ole e 1.0103 protein [Olea europea] (gi|2465129) were identified as nonglycosylated species. These results, partially in disagreement with Swiss-Prot annotation, were validated by matching the MALDI MS/MS spectra of the natural tryptic mixture with those obtained after deglycosylation.