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Identification of the ligand of Pru p 3, a peach LTP

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Abstract

Key message

Pru p 3, a peach LTP, is located in pollinated flower styles and secreting downy hairs, transporting a derivative of camptothecin bound to phytosphingosine. Pru p 3 may inhibit a second pollination and may keep away herbivores until seed maturation.

Abstract

The allergen Pru p 3, a peach lipid transfer protein, has been well studied. However, its physiological function remains to be elucidated. Our results showed that Pru p 3 usually carries a lipid ligand that play an essential role in its function in plants. Using ESI-qToF, we observed that the ligand was a derivative of camptothecin binding to phytosphingosine, wich that is inserted into the hydrophobic tunnel of the protein. In addition, the described ligand displayed topoisomerase I activity inhibition and self-fluorescence, both recognized as camptothecin properties. During flower development, the highest expression of Pru p 3 was detected in the styles of pollinated flowers, in contrast to its non-expression in unpollinated pistils, where expression decreased after anthesis. During ripening, the expression of Pru p 3 were observed mainly in peel but not in pulp. In this sense, Pru p 3 protein was also localized in trichomes covering the fruit epidermis.

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Acknowledgements

The authors thank the Centro de Supercomputación y Visualización de Madrid (CeSViMa) and Centre for Metabolomics and Bioanalysis (CEMBIO) for computing resources and technical assistance. The study was supported by the Ministry of Science and Innovation (project BIO2013-041403-R) and FIS-Thematic Networks and Co-operative Research Centres: RIRAAF (RD12/0013/0014). The funders had no role in the study design, data collection and analysis, the decision to publish, or the preparation of the manuscript.

Author contributions

Sample collection: MH; Experimental design and analysis of results: PGM, MH, LFP, AD-P; Experimental development: NCB, CGC, LT; Modelling and molecular dynamics analysis: MGA, LFP; Confocal microscopy: CRC, PGM.

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Authors and Affiliations

  1. Centre for Plant Biotechnology and Genomics (UPM-INIA), Campus de Montegancedo, 28223, Pozuelo de Alarcón, Madrid, Spain

    Nuria Cubells-Baeza, Carmen Ramírez-Castillejo, María Garrido-Arandia, Pablo González-Melendi, Luis F. Pacios & Araceli Díaz-Perales

  2. Department of Biotechnology-Plant Biology, ETSIAAB, Technical University of Madrid, Madrid, Spain

    Nuria Cubells-Baeza, Carmen Ramírez-Castillejo, María Garrido-Arandia, Pablo González-Melendi & Araceli Díaz-Perales

  3. Department of Experimental Medical Sciences, Lund University, Lund, Sweden

    Cristina Gómez-Casado

  4. Icahn School of Medicine at Mount Sinai, New York, USA

    Leticia Tordesillas

  5. Estación Experimental de Aula Dei (CSIC), Zaragoza, Spain

    María Herrero

  6. Department of Natural Systems and Resources, ETSI Montes, Technical University of Madrid, Madrid, Spain

    Luis F. Pacios

Authors
  1. Nuria Cubells-Baeza
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  2. Cristina Gómez-Casado
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  3. Leticia Tordesillas
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  4. Carmen Ramírez-Castillejo
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  7. María Herrero
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  8. Luis F. Pacios
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  9. Araceli Díaz-Perales
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Correspondence to Araceli Díaz-Perales.

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Cubells-Baeza, N., Gómez-Casado, C., Tordesillas, L. et al. Identification of the ligand of Pru p 3, a peach LTP. Plant Mol Biol 94, 33–44 (2017). https://doi.org/10.1007/s11103-017-0590-z

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  • DOI: https://doi.org/10.1007/s11103-017-0590-z

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