This paper was originally presented at the 26th Informal Meeting on Mass Spectrometry 2008.
Unambiguous characterization and tissue localization of Pru P 3 peach allergen by electrospray mass spectrometry and MALDI imaging†
Article first published online: 10 FEB 2009
Copyright © 2009 John Wiley & Sons, Ltd.
Journal of Mass Spectrometry
Volume 44, Issue 6, pages 891–897, June 2009
How to Cite
Cavatorta, V., Sforza, S., Mastrobuoni, G., Pieraccini, G., Francese, S., Moneti, G., Dossena, A., Pastorello, E. A. and Marchelli, R. (2009), Unambiguous characterization and tissue localization of Pru P 3 peach allergen by electrospray mass spectrometry and MALDI imaging. J. Mass Spectrom., 44: 891–897. doi: 10.1002/jms.1562
- Issue published online: 5 JUN 2009
- Article first published online: 10 FEB 2009
- Manuscript Accepted: 6 JAN 2009
- Manuscript Received: 30 MAY 2008
- SIQUAL (Laboratory for Food Safety and Quality)
- food allergy;
- Pru p 3;
- MALDI imaging;
- LTQ orbitrap
The lipid transfer protein (LTP), Pru p 3, has been identified as the major allergen present in peach, and its sequence obtained by direct amino acid sequencing has been previously reported. However, several sequences, obtained from c-DNA and available in databases, show differences among them and from the originally proposed structure. In this paper, we report the fast and unambiguous determination of the structure of Pru p 3 protein, extracted from three different varieties of peach, by electrospray ionization mass spectrometry (ESI-MS), both coupled to single stage (quadrupole) or advanced (FT-HRMS) analyzers. The structure was identical to one of the cDNA-derived sequences and different in two positions from the previously reported structure obtained by amino acid sequencing. Moreover, the exclusive localization of the protein in the outer part of the fruits was assessed by Matrix-Assisted Laser Desorption Ionization Mass Spectrometry Imaging (MALDI MSI). The results reported here demonstrate the full potential of mass spectrometry for rapidly obtaining high quality structural data of relevant food proteins. Copyright © 2009 John Wiley & Sons, Ltd.