Complete amino acid sequence determination of the major allergen of peach (Prunus persica) Pru p 1

Elide A. Pastorello, Claudio Ortolani, Chiara Baroglio, Valerio Pravettoni, Marco Ispano, Maria Gabriella Giuffrida, Donatella Fortunato, Laura Farioli, Mara Monza, Lorenzo Napolitano, Marco Sacco, Elisabetta Scibola, Amedeo Conti

Research output: Contribution to journalArticlepeer-review

Abstract

The major protein allergen of peach (Prunus persica), Pru p 1, has recently been identified as a lipid transfer protein (LTP). The complete primary structure of Pru p 1, obtained by direct amino acid sequence and liquid chromatography-mass spectrometry (LC-MS) analyses with the purified protein, is described here. The protein consists of 91 amino acids with a calculated molecular mass of 9178 Da. The amino acid sequence contains eight strictly conserved cysteines, as do all known LTPs, but secondary structure predictions failed to classify the peach 9 kDa protein as an 'all-alpha type', due to the high frequency of amino acids (nine prolines) disrupting alpha helices. Although the sequence similarity with maize LTP is only 63%, out of the 25 amino acids forming the inner surface of the tunnel-like hydrophobic cavity in maize ns-LTP 16 are identical and 7 similar in the peach homolog, supporting the hypothesis of a similar function.

Original languageEnglish
Pages (from-to)1315-1320
Number of pages6
JournalBiological Chemistry
Volume380
Issue number11
Publication statusPublished - Nov 1999

Keywords

  • Lipid transfer protein
  • Primary structure
  • Rosaceae

ASJC Scopus subject areas

  • Biochemistry

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